sidA

L-ornithine N(5)-monooxygenase

501 amino acids

L-ornithine N(5)-monooxygenase; part of the siderophore biosynthetic pathway (PubMed:26960149). Arthroderma benhamiae produces 2 types of extracellular siderophores, ferrichrome C and ferricrocin (PubMed:26960149). The biosynthesis of these siderophores depends on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed by the monooxygenase sidA (PubMed:26960149). The structure of ferricrocin differs from ferrichrome C only by a serine for alanine substitution and the assembly of both siderophores is suggested to be performed by the nonribosomal peptide synthase (NRPS) sidC (PubMed:26960149).

Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.

56.173 kDa

MNGTSTTGNGFTNGTNYPVPKLELQPETTSTSPTRAQTHPLLPSVSDDELHDLICVGFGPASLAIAIALHDRLLETAHSPDITTVPKICFLEKQSNFAWHSGMLLPGSKMQISFIKDLATIRNPRSEFTFLNYLQVHDRLLDFANLGTFLPARIEFEDYMKWCASKFANLVRYRTEVLDVTPSEVDPVTGKVHFFTVRSKVLETGEVTTRKARHVVVAIGGKPNIPAEFPTNSRIIHSSAYCTTLPSLLNNTLKEYSIAVAGSGQSAAEIFHDLQKRYPNAKTSLIMRDSALRPSDDSPFPSVNELFNPERVDQFFNQSEKERQHFLERHRSTNYSVVRPELIEQIYADMYIQKIQYPDETQWQHRIFSSCLISKVDSDKSEKLNLSLQHCHSENTTMNGTHNEEMNADALILATGYVRNAHESILASIEPLLAQKHMGWKVQRNYRLELDKNQVDVDAGIWLQGCNESTHGLSDSLLSILAVRGAEIVQAIFGAQISNGN

sidA

L-ornithine N(5)-monooxygenase

501 amino acids

L-ornithine N(5)-monooxygenase; part of the siderophore biosynthetic pathway (PubMed:15504822, PubMed:16113265, PubMed:17845073, PubMed:20614882, PubMed:20650894, PubMed:22465572). Aspergillus fumigatus produces four types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (FsC) and triacetylfusarinine C (TAFC) for iron uptake; and intacellular ferricrocin (FC) for hyphal and hydroxyferricrocin (HFC) for conidial iron distribution and storage. TAFC consists of three N(2)-acetyl-N(5)-anhydromevalonyl-N(5)-hydroxyornithine residues cyclically linked by ester bonds; FC is a cyclic hexapeptide with the structure Gly-Ser-Gly-(N(5)-acetyl-N(5)-hydroxyornithine)x3. The biosynthesis of all four siderophores depends on the hydroxylation of ornithine, catalyzed by the monooxygenase sidA (PubMed:15504822, PubMed:16113265, PubMed:20614882, PubMed:20650894, PubMed:22465572). SidA is highly specific for its substrate, only hydrolyzing l-ornithine, and has preference for NADPH over NADH, NADPH playing a role in stabilization of the C4a-hydroperoxyflavin intermediate (PubMed:20614882, PubMed:22465572). Subsequently, the pathways for biosynthesis of extra- and intracellular siderophores split (PubMed:17845073). For biosynthesis of extracellular siderophores, the transacylase sidF transfers anhydromevalonyl to N(5)-hydroxyornithine (PubMed:17845073). The required anhydromevalonyl-CoA moiety is derived from mevalonate by CoA ligation and dehydration catalyzed by sidI and sidH respectively (PubMed:22106303). The acetylation of N(5)-hydroxyornithine for FC biosynthesis involves the constitutively expressed sidL (PubMed:21622789). FC is hydroxylated to HFC by an as yet uncharacterized enzyme during conidiation (PubMed:17845073). Assembly of fusarinine C (FsC) and FC is catalyzed by two different nonribosomal peptide synthetases (NRPS), sidD and sidC respectively (PubMed:17845073). Subsequently, sidG catalyzes N2-acetylation of FsC for forming TAFC (PubMed:17845073). Both extra- and intracellular siderophores are crucial for growth during iron limitation and virulence (PubMed:16113265).

Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.

56.877 kDa

MESVERKSESSYLGMRNMQPEQRLSLDPPRLRSTPQDELHDLLCVGFGPASLAIAIALHDALDPRLNKSASNIHAQPKICFLERQKQFAWHSGMLVPGSKMQISFIKDLATLRDPRSSFTFLNYLHQKGRLIHFTNLSTFLPARLEFEDYMRWCAQQFSDVVAYGEEVVEVIPGKSDPSSSVVDFFTVRSRNVETGEISARRTRKVVIAIGGTAKMPSGLPQDPRIIHSSKYCTTLPALLKDKSKPYNIAVLGSGQSAAEIFHDLQKRYPNSRTTLIMRDSAMRPSDDSPFVNEIFNPERVDKFYSQSAAERQRSLLADKATNYSVVRLELIEEIYNDMYLQRVKNPDETQWQHRILPERKITRVEHHGPQSRMRIHLKSSKPESEGAANDVKETLEVDALMVATGYNRNAHERLLSKVQHLRPTGQDQWKPHRDYRVEMDPSKVSSEAGIWLQGCNERTHGLSDSLLSVLAVRGGEMVQSIFGEQLERAAVQGHQLRAML

sidA

L-ornithine N(5)-monooxygenase

498 amino acids

Catalyzes the conversion of L-ornithine to N(5)-hydroxyornithine, the first step in the biosynthesis of all hydroxamate-containing siderophores, such as the secreted triacetylfusarinine C (TAFC) involved in iron uptake and the intracellular iron storage compound desferriferricrocin (DFFC).

Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family.

56.562 kDa

MEPLQRKSELDFQSYRKMPLAQQRTQRLKPTSPEELHDLICVGFGPASLAIAIALHDALDPCLNKCAPTSGWQPKVAFLERQKQFAWHSGMLVPGSRMQISFIKDLATLRDPRSSFTFLNYLHQKDRLIHFTNLSTFLPARMEFEDYMRWCANQFSDVVTYGEEVIEVLPGKSSPDSPVVDYFTVLSRNVETGEISSRSARKVVLALGGTAKLPAELPQDPRIMHSSKYCTALPNLLKDNNEPYNIAVLGSGQSAAEIFHDLQKRYPNSRTSLIMRDTAMRPSDDSPFVNEVFNPERTDKFYNLSAAERERSLKADKATNYSVVRLELIEEIYHDMYLQRVKNPDETQWQHRILPSRKITRVEHYGPNKRMRVHVRAVKDGKDSLIGDGKEVLEVDALMVATGYNRNAHEQLLSKVQYLRPATQDRWTPSRDYRVDLDRSKVSAGAGIWLQGSNEQTHGLSDSLLSVLATRGGEMVESIFGEQLESAAVPDTRFRAML

sidA

Cell division inhibitor SidA

29 amino acids

Inhibits cell division by binding directly to FtsW to prevent the final constriction of the FtsZ ring.

3.215 kDa

MIRVARESFALVSVIGFVWMMCTVANLVA