About Products Protein Database Contact

lpsB

Gene
lpsB
Protein
D-lysergyl-peptide-synthetase subunit 2
Organism
Epichloe festucae var. lolii
Length
1351 amino acids
Function
D-lysergyl-peptide-synthetase subunit 2; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid ergovaline, the predominant ergopeptine product in E.festucae var. lolii (PubMed:17308187). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (By similarity). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (By similarity). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (By similarity). The presence of easA is not required to complete this reaction (By similarity). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (By similarity). Paspalic acid is then further converted to D-lysergic acid (By similarity). Ergovaline is assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetase composed of a monomudular (lpsB) and a trimodular (lpsA) nonribosomal peptide synthetase subunit (PubMed:17308187, PubMed:11592979).
Similarity
Belongs to the NRP synthase family.
Mass
147.939 kDa
Sequence
MQSQVRLPSNGNPALSFPQNEIGGPVHWKTYLEGCSPCSFPSLRTVCPSQSWPASVSITIGDSIFRRLEHFSDKTGISVATVFRASWGLVLRIYTGQDSVCFGDMTTAPGGIDAIGCVGVCRVELSDTAVISKVLQRIQAASANKLAIPHVPLSDAVLSKCMPSASLFNTCMLISGGGERPEKTSSTFEKVELGYDDQYDIIVRGSVEDSGASAALSYRTSFLSEEQATSIANTFERAVSDLIGIENRIGQICFLSDLDKSQIYTWNKDPPLRAHSCVDTLIHERCLSQPTASAVNAWDGELSYEELNHLSSKLSRHLVTLGVGAEVFVPLCFEKSRWTTVAMLAVIKAGGAFVLLDPSHPAERLLSICQKVSARLIVASAQHAKLAEDLVTSIVEVGDDKADWLTDKGIKAQTQTRTRRSAAPGDALYAVFTSGSTGTPKGVIIEHGSFHAAVFPYTEAVGLNQESRVFQFSSYAFDVTIFDTLMTLISGGCVCVPSNTERWSDVANAIQRFRVTHSSLTPTVARILDPKDVLTLRTLVLGGEKLVTSDITKWVDQVRLVHLYGASECPIMSIQSMTGVASDFQTTDHATGSNCWIVDPNNHDRLVPIGTIGELVIEGTIVGRGYLDDPEKSSATFIRPPGWLCQVRGSGYHSAVYKSGDLVQYTADGSLRYIGRKDTQVKLRGQRVELGEVEHHVKLTFPNATDVVVELVVTIHASSSRAPILVAFVLISHEADPDPESIRTGRGEGLSQILSEPTDRFCSQIPIVQSQLQQSLPSYMVPGIFLPLMTLPLTSTDKINRKLLRELAGALSREELESYQPSTGPVRAPQTTTEKLLQQYFARVLNIPVEQVGADDHFFQRGGDSLTAMKLVAMARKDKHKLTVQDIFDSPRLSALACVVRSGKVDGNKEPPLEPFSLVNKHRDIIRAAAQQCQLPVRVIEDVYPCTPLQRGLISETLRDSKAFIAHLAVSLPPDIDLQRLQEAWTTVANANPILRTRMVLSASHGLLQVVVREDIRWIVSKNAEAQDFFVGVGKPLVQLVLCCHREGNEVPVQLLLMVHHAVYDGYTLPLIFEQVKAAYNGGTLAPRPAVPFIRYVQSIPDGTGYWNSLMANLQTPIFPALPSKSYQPLPNAIMRHTIITPGSHRQYTPSTYVRLAWAITQAYHQGTCDIFFGTVVSGRNAPVTDIELMTIPTVATIPCRVTLDFQSLVQSALRKIQDDAISGIPFEQLGLPHIRRLGEHAMLACSFQTLLSIQPALPPSTDAWFEQPGSTIDYRANATYAINLFFGLEGDKLKATALYDFNVVKKDKMQSMLVDFGNILQTMHKSPNSLIRDILAVPQQMRGPINSASL

Gene
lpsB
Protein
D-lysergyl-peptide-synthetase subunit 2
Organism
Claviceps purpurea
Length
1308 amino acids
Function
D-lysergyl-peptide-synthetase subunit 2; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:10071219, PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187, PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by EasD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20118373, PubMed:21409592). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (PubMed:20735127, PubMed:21494745). The presence of easA is not required to complete this reaction (PubMed:21494745). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:16538694, PubMed:17720822). Paspalic acid is then further converted to D-lysergic acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent dioxygenase easH which introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group (PubMed:24361048).
Similarity
Belongs to the NRP synthase family.
Mass
143.85 kDa
Sequence
MATPEKWRKYLEDYIPCSFPTFLDNEGADSKSFASVLVRLEHPYGRLMSFSNNCGVDVAVVLNVAWGIVLQAYTGQDATCFAVIAESNLNIRPCRIRFTSDKVVSDILSACQSPCSEKTGDHDIPASHLSQDGGFLASEFFNTCIWGPMQGSQMTSETQAADMNRNALNLFDLVTRVEVPRVEVDKSITRITLTYKRGLMREHQALAVAKAMERAISEIISGKERLDQFCLLTSEDRRQMSLWNMNLSDNSDARIETLIHEWCRRTPSAVAVCGWDGDFSYKELNELSTGVKHDLRHLGIGPEVFVPILFEKSRWAVIAMLGVMKAGGAFILLDPAHPPKRLRSICDKVSARLVVSSVQQADLAAGLAGHVVIVGGEVATAGMAQHVGEHDDSMDCIAAPHNALYAVFTSGSTGTPKGVVNSHSSFLAAMPVYLKALELDNNSRVFQFASYAFDVTIFDALMTLVAGGCVCVLSNADRSSDLTSAIQHFGTTHLSVTPTVARILDPQDFPSLKTIVLGGELSASDELLKWVNNVRVIRLYGASECTVMSIQCTSGPASSIKTINYETGNCCWVVNPQNHEQLRPLGAVGELLVEGAVVGRGYLDDASQTSETFIEAPAWLQELRQGSSTVYKSGDLVRIAADKSVQFVCRKSTQVKLRGQRIELGEVEHHVRLAIPSATECVVELITIPDASRPPMLMAFVLSDTDASTSSITARRNATSDAVFAEPSASFRSQIASITSKLRDALPSYMVPSVILPLRIMPLTGTDKINRKLLRQLAAALSREDLQLYQAQQTTYRAPSNDIEEAFQRFFAQALGLSLDQIGADDHFFSLGGDSLTAMRLAAMARKAKFDLTVQNVFDHPELSELARHTKLVADESQEFPQPFTLIAGSKQGIVRDAARQCRLPSRVIEDVYPCTPLQKGLLAETMRDAAAFVAKIEVPLPRDVDLDRLRQAWAAVAKANPILRTRMIFSPSYGMLQVVVREDVPWIESDEVESQELVVVGRSLVQLILRRRPSTALFLHIHHAVYDGYSLPLMFAQLNNAYHGETLAFRPASAFIRYLATMPDATDYWQSMCQGLESPSFPALPHPSHRPHPDSKATHTVCVASPHAREYTPNTHVRLAWAITQAHEQGLLDVFYGTVVSGRNAPVDQIESMLIPTVATVPCRITLDVDSPVRKILHRIQDVATRGIPFEQIGLAEISHLGKDAAHACSFQTLLLMQPTAVEQNENDFFNTSTSDANYRADATYAINLFCTLENQDLSVTALYDGNIVSTDTMQRLLQNLGKSMQEIHAAPRTLIGDILKSLHSRL

Gene
lpsB
Protein
D-lysergyl-peptide-synthetase subunit 2
Organism
Claviceps purpurea (strain 20.1)
Length
1303 amino acids
Function
D-lysergyl-peptide-synthetase subunit 2; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:10071219, PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187, PubMed:17720822). DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265). The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20118373, PubMed:21409592). Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (PubMed:20735127, PubMed:21494745). The presence of easA is not required to complete this reaction (PubMed:21494745). Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:16538694, PubMed:17720822). Paspalic acid is then further converted to D-lysergic acid (PubMed:15904941). Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit (PubMed:14700635, PubMed:15904941). LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone (PubMed:14700635). LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines (PubMed:14700635). LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea (PubMed:17560817, PubMed:19139103). D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048). Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent dioxygenase easH which introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group (PubMed:24361048).
Similarity
Belongs to the NRP synthase family.
Mass
143.112 kDa
Sequence
MATPEKWRKYLEDYIPCSFPTFLDNEGADSKSFASVLVRLEHPYGRLMSFSNNCGVDVAVVLNVAWGIVLQAYTGQDATCFAVIAESNLNIRPCRIRFTSDKVVSDILSACQSPCGEKTGDHDIPASHLSQDGGFLASEFFNTCIWGPMQGSQMPSETQAADMNRNALNLFDLVTRVEVDKSITRITLTYKRGLMREHQALAVAKAMERAISEIISGKERLDQFCLLTSEDRRQMSLWNMNLSDNSDARIETLIHEWCRWTPSAVAVCGWDGDFSYKELNELSTGVKHDLRHLGIGPEVFVPILFEKSRWAVIAMLGVMKAGGAFILLDPAHPPKRLRSICDKVSARLVVSSVQQADLAAGLAGHVVIVGGEVATAGMAQHVGEHDDSMDCIAAPHNALYAVFTSGSTGTPKGVVNSHSSFLAAMPVYLKALELDNNSRVFQFASYAFDVTIFDALMTLVAGGCVCVPSNADRSSDLTSAIQHFGTTHLSVTPTVARILDPQDFPSLKTIVLGGELSASDELLKWVNNVRVIRLYGASECTVMSIQCTSGPASSIKTINYETGNCCWVVNPQNHEQLRPLGAVGELLVEGAVVGRGYLDDASQTSETFIEAPAWLQELRQGSSTVYKSGDLVRIAADKSVQFVCRKSTQVKLRGQRIELGEVEHHVRLAIPSATECVVELITNPDASRPPMLMAFVLSDTDASTSSITARRNATSDAVFAEPSASFRSQIASITSKLRDALPSYMVPSVILPLRIMPLTSTDKINRKLLGQLAAALSREDLQLYQAQQTTYRAPSNDIEEAFQRFFAQVLGLSLDQIGADDHFFSLGGDSLTAMRLAAMARKAKFDLTVQNVFDHPELSELARHTKLVADESQEFPPPFTLVAGSKQGIVRDAARQCRLPSRVIEDVYPCTPLQKGLLAETMRDAAAFVAKIEVPLPRDVDLDRLRHAWAAVAKANPILRTRMIFSPSYGMLQVVVREDIPWIESDDVESQELVAVGRSLVQLILRRRPSTALFLHIHHAVYDGYSLPLMFAQLNNAYHGETLAFRPASAFIRYLATMPDATDYWQSMCQGLESPSFPALPHSSHRPHPDSKATHTVCVASPQAREYTPNTHVRLAWAITQAHEQGLLDVFYGTVVSGRNAPVDQIESMLIPTVATVPCRISLDVDSPVRKILHRIQDVATRGIPFEQIGLAEISHLGKDAAHACSFQTLLLMQPTAVEQNENDFFNTSTSDANYRADATYAINLFCTLENQDLSVTALYDGNIVSTDTMQRLLQNLGKSMQEIHAAPRTLIGDILKSLHSRL

Gene
lpsB
Protein
Lipopolysaccharide core biosynthesis mannosyltransferase LpsB
Organism
Rhizobium meliloti (strain 1021)
Length
351 amino acids
Function
Acts at transfer of mannose group to a 3-deoxy-D-mono octulonic acid (KDO) via an alpha-1,5 linkage.
Similarity
Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.
Mass
38.662 kDa
Sequence
MVDIRDVEVIAPNFKQRLSGVTSTIIQLVPVQRALGQKIAVLGPGLPKSLPSVRFRDLIHLWKRPEGRPCRVWHARRNVEMLPAILLRDLLRMKLRIVFTSASQRRHTGWSKFLIRRMDAVIATSGRTAAYLDVPNTVILHGIDTKRFQPPFDKTEAKKALGLDPAKKFVGCFGRVRHQKGTDLFVDSMIALLPCRPDWGAIVAGRATGPHLAFESELKERVAKAGLADRILFVGEHTNIPDWYRALDLFVAPQRWEGFGLTPLEAMATGVPVVATDVGAFSELVTGGSEETGLIIAADDLKAMVDAAAAFMDDRPRLAAASANGLARTSKNFAIEQEARAIAAVYESLMR