ID A0A0L0HET9_SPIPD Unreviewed; 699 AA.
AC A0A0L0HET9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000256|ARBA:ARBA00018612};
DE EC=1.14.13.196 {ECO:0000256|ARBA:ARBA00012881};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000256|ARBA:ARBA00030351};
GN ORFNames=SPPG_04897 {ECO:0000313|EMBL:KNC99504.1};
OS Spizellomyces punctatus (strain DAOM BR117).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Spizellomycetaceae; Spizellomyces.
OX NCBI_TaxID=645134 {ECO:0000313|EMBL:KNC99504.1, ECO:0000313|Proteomes:UP000053201};
RN [1] {ECO:0000313|EMBL:KNC99504.1, ECO:0000313|Proteomes:UP000053201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM BR117 {ECO:0000313|EMBL:KNC99504.1,
RC ECO:0000313|Proteomes:UP000053201};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine +
CC NAD(+); Xref=Rhea:RHEA:41512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78275; EC=1.14.13.196;
CC Evidence={ECO:0000256|ARBA:ARBA00001398};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine +
CC NADP(+); Xref=Rhea:RHEA:41508, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78275; EC=1.14.13.196;
CC Evidence={ECO:0000256|ARBA:ARBA00001847};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000256|ARBA:ARBA00007588}.
CC -!- SIMILARITY: Belongs to the lysine N-acyltransferase MbtK family.
CC {ECO:0000256|ARBA:ARBA00009893}.
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DR EMBL; KQ257457; KNC99504.1; -; Genomic_DNA.
DR RefSeq; XP_016607544.1; XM_016753136.1.
DR AlphaFoldDB; A0A0L0HET9; -.
DR STRING; 645134.A0A0L0HET9; -.
DR GeneID; 27688323; -.
DR VEuPathDB; FungiDB:SPPG_04897; -.
DR eggNOG; KOG1399; Eukaryota.
DR InParanoid; A0A0L0HET9; -.
DR OMA; YHGNTNY; -.
DR OrthoDB; 1422935at2759; -.
DR Proteomes; UP000053201; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR019432; Acyltransferase_MbtK/IucB-like.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR025700; Lys/Orn_oxygenase.
DR PANTHER; PTHR42802:SF1; L-ORNITHINE N(5)-MONOOXYGENASE; 1.
DR PANTHER; PTHR42802; MONOOXYGENASE; 1.
DR Pfam; PF13523; Acetyltransf_8; 1.
DR Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR PRINTS; PR00368; FADPNR.
DR SMART; SM01006; AlcB; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053201}.
FT DOMAIN 538..585
FT /note="Acyltransferase MbtK/IucB-like conserved"
FT /evidence="ECO:0000259|SMART:SM01006"
SQ SEQUENCE 699 AA; 78247 MW; 2172F9C8C0977C26 CRC64;
MPATQSQPEQ FDVLCVGFGP AGLAIAAAMA DEKVISLDTT TADESLRVRF IEKQPSFLWH
GGMLLDGTKM QISFLKDLAT LRDPTSNFTF LKYLHENDRL VPFVNLGTWN PYRVEFNDYL
SWAAKKFEKF CDYGEQVMSV DPLIHPQDGT VSQLRVTSRT SDGARIVRDT KNIIVAIGGQ
PRYPDFVHRS IGSQVDQTTT PHLAHTSQYT YRVQQMLPDA EASYRLAVIG SGQSAAEVFM
DLGRRYPNAE VNLIFRDSAL RPSDDSPFVN EVFDPDRRDA FYAQTSEQRK SSLIRDKATN
YSVVNENLIN EIYGMMYMQR LPGSETRPKH ALMPNHSILD MHKSSGGITL TLRDSRSDNT
TGYERTFDAV FLGTGYERFA HLDVLQPVLP YLNKDQDNKI VVGRDYRVST TNACRAGIYV
QGCCEDTHGL SDTLLSVLGV RGGEVLQSIQ ARMNKVQILG QKQSGNMVDV KQTATPPASP
VPSPTTCQRI NVDRIDSGIN VTGTKKESGL APCPPKPLPG TILFSKYIPH LNETFSLRVA
NLQTDIPLLT KWHNNPRVSK FWNEVGDESH HTKYLSTLLA DPHSIPCIGM FNDVPFAYFE
IYWAAHDRLA GYYDAGTHDR GFHLLVGEEA YRGSHRVEGW LPAVVEFMFG DCSGTKRVVL
EPRADNGKLI GYLCNFGFQF KGEIKLPHKT AALMVMETE
//
