ID A1CKH2_ASPCL Unreviewed; 593 AA.
AC A1CKH2;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
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=ACLA_038570 {ECO:0000313|EMBL:EAW09646.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW09646.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW09646.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR EMBL; DS027056; EAW09646.1; -; Genomic_DNA.
DR RefSeq; XP_001271072.1; XM_001271071.1.
DR AlphaFoldDB; A1CKH2; -.
DR EnsemblFungi; EAW09646; EAW09646; ACLA_038570.
DR GeneID; 4703472; -.
DR KEGG; act:ACLA_038570; -.
DR VEuPathDB; FungiDB:ACLA_038570; -.
DR eggNOG; ENOG502QPIW; Eukaryota.
DR HOGENOM; CLU_014633_1_1_1; -.
DR OMA; ACHSMQI; -.
DR OrthoDB; 5491437at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR025700; Lys/Orn_oxygenase.
DR PANTHER; PTHR38663; -; 1.
DR PANTHER; PTHR38663:SF1; ZGC:113276; 1.
DR Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT REGION 62..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 66380 MW; 07D92C5B28A0C169 CRC64;
MPPLHDVLII GAGPCALAVA ARLHEPTPSA MFTDEEHQRY HWINKHSGRM ALVQAQRRKL
NGVRAEPWRA HASKRRTSDS SSASGAPASI SAASSVPSLA SSLSPSSVDM DTDMSGEKRL
GARRESGVSV LVLDGTGERW MQRWETAFRT LEIAQLRSPM FFHVDPGDRD GMLAYARETG
READLWEIGG CVGKEVSKHK RKKRMRARAV AMGETEIDER DRKDYFSPST GLFADYCASI
VERYGLNAPG MILQREVGDI QYDYDDEISP YEKIFTVTAS DGSRFYSRAV VLAIGPGKTK
MLPFELSADE RMGACHSTEI RAFPSPNVKR KMQQREETNV VVVGGGLSSA QIVDMAVRKG
VTKVWFIMRS DFKVKHFDFG LTWVGKFKNY EKAAFWSADT DDERLEMIKV ARNGGSITPR
YQKIVKQHAA RNRVSIHTRT VICDKEYCPL TQTWRLTTDP PIPDLPPIDY IYFATGMKCD
VQEMPLLQRM HRDYPIETKQ GLPCITDDLM WQPGVPLFVT GRLASLRLGP AAPNLEGARL
GAERIAWAME DVLGRKEAED DEVGRSRQCF CGLGNRYAEL SVHADADNDF DCL
//
