malP

Maltodextrin phosphorylase

831 amino acids

Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Catalyzes the phospholytic cleavage of maltodextrins with a minmal chain length of five glucose residues to yield glucose-1-phosphate. Low activity with tetraose and no activity with triose and maltose. Long maltodextrins (8 to 15 glucose units), amylose and starch are not as good substrates as maltoheptaose.

Belongs to the glycogen phosphorylase family.

96.683 kDa

METVVNQIKSKLPENLEGLLDLAYNYWWSWNRRATKLWEKIDPEHWWEYKNPVKLLLDTPEERLKELSKDDDFINLYELVIDQFRHYMNPESTWFSTNYPKWEEPVIYLCMEYGISKSLPIYSGGLGILAGDHIKTASDLGIPLIAIGLLYKHGYFKQEIDKDGKQIEVFPEYNPEEMPIKPLTTEKGKPLLIEVPIEDRIVYARAFEVNVGRVKLYLLDTDVPQNSPDDRTICDYLYNAEIDKRIKQEILLGIGGMRLLRMLGIDPAVIHLNEGHPAFANFQRIAWYMEEGLNFLEALTVVRGTTIFTTHTPVPAGHDKFPIAEVEKRLAKFLEGLPKDEFLNLGREGDQFNMTLLSIRTSSYVNAVSKLHSKVTKEMWRHLWNGVPLDEIPVEGITNGVHTKTWLHNEIKKLVDRYIGRVWRDYAELEGLWYGVERIPDEELWEAHLKAKREFIELIKRKIKERNERLGIEEPLPEIDENALIIGFARRFATYKRATLILTDLERLKKIVNNPERPVYIIFGGKAHPRDEAGKEFLRKVYEVSQMPEFKNKIMVFENYDMGSARAMVAGVDVWLNNPRRPLEASGTSGMKAGLNGVLNLSVYDGWWVEGYNGKNGWVIGDESLEPETEKDNIRDAQSLYNLLENEVIPTYYENRARWIYMMKESIKSIAPRFSTHRMVKEYVDKFYSKALANAILLQRDSFKATREIASWKAKIFNSWDKVEIERIITHDATGVEVIVNLDGLSPEDVKVEIYYGVKAEGYAIEKPYVIELKHPQSLGGNRWLYRYEGNALKNLGHPCWHYAVRVYPYHDKLPHKFLLGLIKWKGFFEL

malP

Maltodextrin phosphorylase

797 amino acids

Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

Belongs to the glycogen phosphorylase family.

90.522 kDa

MSQPIFNDKQFQEALSRQWQRYGLNSAAEMTPRQWWLAVSEALAEMLRAQPFAKPVANQRHVNYISMEFLIGRLTGNNLLNLGWYQDVQDSLKAYDINLTDLLEEEIDPALGNGGLGRLAACFLDSMATVGQSATGYGLNYQYGLFRQSFVDGKQVEAPDDWHRSNYPWFRHNEALDVQVGIGGKVTKDGRWEPEFTITGQAWDLPVVGYRNGVAQPLRLWQATHAHPFDLTKFNDGDFLRAEQQGINAEKLTKVLYPNDNHTAGKKLRLMQQYFQCACSVADILRRHHLAGRKLHELADYEVIQLNDTHPTIAIPELLRVLIDEHQMSWDDAWAITSKTFAYTNHTLMPEALERWDVKLVKGLLPRHMQIINEINTRFKTLVEKTWPGDEKVWAKLAVVHDKQVHMANLCVVGGFAVNGVAALHSDLVVKDLFPEYHQLWPNKFHNVTNGITPRRWIKQCNPALAALLDKSLQKEWANDLDQLINLEKFADDAKFRQQYREIKQANKVRLAEFVKVRTGIEINPQAIFDIQIKRLHEYKRQHLNLLHILALYKEIRENPQADRVPRVFLFGAKAAPGYYLAKNIIFAINKVADVINNDPLVGDKLKVVFLPDYCVSAAEKLIPAADISEQISTAGKEASGTGNMKLALNGALTVGTLDGANVEIAEKVGEENIFIFGHTVEQVKAILAKGYDPVKWRKKDKVLDAVLKELESGKYSDGDKHAFDQMLHSIGKQGGDPYLVMADFAAYVEAQKQVDVLYRDQEAWTRAAILNTARCGMFSSDRSIRDYQARIWQAKR

malP

Maltose phosphorylase

783 amino acids

Catalyzes the phosphorolysis of maltose, leading to the formation of glucose and glucose 1-P. Does not have maltose 6'-P phosphorylase activity. Plays an important role in the metabolism of maltose taken up via the bacterial phosphotransferase system (PTS).

Belongs to the glycosyl hydrolase 65 family.

90.212 kDa

MQSVAFMIDLSIKSLRGILMKQIKRLFQIDPWKIRTTHLDKENLRLQESLTSIGNGYMGMRGNFEEHYSGDHHQGTYLAGVWYPDKTRVGWWKNGYPEYFGKVINAINFIAMDLQIDGQTIDLATTPYEDFSLELDMQNGVLSRQFTIQTPKNKVRFSFERFLSLEKKEAAYIHLTIEMLEGTGTITLHSKLDGDVQNEDSNYEEHFWEEIAIETQETLGFVTTKTIPNNFEIERFTVTAGMRHFIDGASVVPTYTQQPLALTAELTVSLNEGETTAITKEVLVVTSRDVPETQQITRVNELFSEMTTLYPEAKAGQAAAWAKRWQLADVVIEGDDEAQQGIRFNLFQLFSTYYGEDDRLNIGPKGFTGEKYGGATYWDTEAYAVPLYLALAKPEVTKNLLKYRHNQLPQAIHNAQQQGLKGALYPMVTFTGVECHNEWEITFEEIHRNGAIAYAIYNYVNYTGDQDYLKDAGLEVLVAIARFWADRVHFSQRHKQYMIHGVTGPNEYENNINNNWYTNTIAAWVLRYTRESYLKFQEETTLKIADDELAKWADIVENMYFPVDNELGIFVQHDTFLDKDLMPVSDLPLSELPLNQHWSWDKILRSCFIKQADVLQGIYFFNDAFSLEEKRRNFNFYEPMTVHESSLSPSIHAVLAAELGMEEKAVEMYQRTARLDLDNYNNDTEDGLHITSMTGSWLAIVQGFAQMKTDHQQLKFAPFLPATWTAYSFHINYRNRLLFVEVAADQVAFTLLDGPAIPLTVYDQKYTLKDRLVLPIRKEEVHV

malP

Maltodextrin phosphorylase

752 amino acids

Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

Belongs to the glycogen phosphorylase family.

85.202 kDa

MLSLQEFVQNRYNKTIAECSNEELYLALLNYSKLASSQKPVNTGKKKVYYISAEFLIGKLLSNNLINLGLYDDVKKELAAAGKDLIEVEEVELEPSLGNGGLGRLAACFIDSIATLGLNGDGVGLNYHFGLFQQVLKNNQQETIPNAWLTEQNWLVRSSRSYQVPFADFTLTSTLYDIDVTGYETATKNRLRLFDLDSVDSSIIKDGINFDKTDIARNLTLFLYPDDSDRQGELLRIFQQYFMVSNGAQLIIDEAIEKGSNLHDLADYAVVQINDTHPSMVIPELIRLLTARGIDLDEAISIVRSMTAYTNHTILAEALEKWPLEFLQEVVPHLVPIIEELDRRVKAEYKDPAVQIIDESGRVHMAHMDIHYGYSVNGVAALHTEILKNSELKAFYDLYPEKFNNKTNGITFRRWLMHANPRLSHYLDEILGDGWHHEADELEKLLSYEDKAVVKEKLESIKAHNKRKLARHLKEHQGVEINPNSIFDIQIKRLHEYKRQQMNALYVIHKYLDIKAGNIPARPITIFFGGKAAPAYTIAQDIIHLILCMSEVIANDPAVAPHLQVVMVENYNVTAASFLIPACDISEQISLASKEASGTGNMKFMLNGALTLGTMDGANVEIAELVGEENIYIFGEDSETVIDLYAKAAYKSSEFYAREAIKPLVDFIVSDAVLAAGNKERLERFYNELINKDWFMTLLDLEDYIKVKEQMLADYEDRDAWLDKVIVNISKAGFFSSDRTIAQYNEDIWHLN

malP

PTS system maltose-specific EIICB component

527 amino acids

The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in maltose transport.

58.055 kDa

MMQKIQRFGSAMFVPVLLFAFAGIIVGISTLFKNKTLMGPLADPDGFWYQCWYIIEQGGWTVFNQMPLLFAIGIPVALAKKAQARACLEALTVYLTFNYFVSAILTVWGGAFGVDMNQEVGGTSGLTMIAGIKTLDTNIIGAIFISSIVVFLHNRYFDKKLPDFLGIFQGSTYIVMISFFIMIPIALAVSYIWPMVQSGIGSLQSFLVASGAVGVWIYTFLERILIPTGLHHFIYTPFIYGPAVAEGGIVTYWAQHLGEYSQSAKPLKELFPQGGFALHGNSKIFGIPGIALAFYVTAKKEKKKLVAGLLIPVTLTAIVAGITEPIEFTFLFISPFLFAVHAVLAATMSTVMYMAGVVGNMGGGLIEAVTLNWIPLFGSHGMTYVYQILIGLSFTAIYFFVFRFLILKFNIATPGREKDEQQETKLYSKKEYRERKNKDETASAAETADDTAFLYIEALGGKDNITEVTNCATRLRVSVKDETKVEPDSVFRALGAHGVVRNGKAFQVIIGLSVPQMRERVEKILNQ

malP

Maltodextrin phosphorylase

108 amino acids

Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.

Belongs to the glycogen phosphorylase family.

12.325 kDa

single

MSQTSFNKAQFQAALTRQWQHFGLQSASEMTQRQWWRAVSGALSELLSAQPVAKATEGERHVNYISMEFLIGRLTGNNLLNLGWYQQVSDELQAHDVNLTDLLEEEID