ID A0A127MFJ9_9SPHN Unreviewed; 863 AA.
AC A0A127MFJ9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Steroid monooxygenase {ECO:0000313|EMBL:AMO72062.1};
GN ORFNames=AZE99_09565 {ECO:0000313|EMBL:AMO72062.1};
OS Sphingorhabdus sp. M41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingorhabdus.
OX NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO72062.1, ECO:0000313|Proteomes:UP000073959};
RN [1] {ECO:0000313|EMBL:AMO72062.1, ECO:0000313|Proteomes:UP000073959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:AMO72062.1,
RC ECO:0000313|Proteomes:UP000073959};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00010139}.
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DR EMBL; CP014545; AMO72062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127MFJ9; -.
DR STRING; 1806885.AZE99_09565; -.
DR KEGG; sphg:AZE99_09565; -.
DR OrthoDB; 312624at2; -.
DR Proteomes; UP000073959; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR43098; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR PANTHER; PTHR43098:SF3; L-ORNITHINE N(5)-MONOOXYGENASE-RELATED; 1.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR Pfam; PF13738; Pyr_redox_3; 1.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000313|EMBL:AMO72062.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 629..831
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
SQ SEQUENCE 863 AA; 94240 MW; 85D09911C6D88DD0 CRC64;
MERNMVEAAG RKFDIVVVGA GFAGLYLLHK FRQMGLSAHA FEAGDDVGGT WYWNRYPGAR
CDIESIDYSF SFDPELEQEW EWSEKYATQP EILRYAQHVA ERFDLRRDIT FEARVETAVW
DEDASSWTVT TETGETVSSR FFIMATGCLS QPKDIDIEGI ENFAGEIYRT HSWPHEGVDF
SGKRVGVIGT GSSGIQSIPL IAEQADSTTV FQRTANYSLP AGNGPIAPEK LAVKKRYQDY
REEARWTKVG VPGKEAMDFA LTVSDEERQQ RYEKLWNTGA IPHLGSEFAD ILLDEQANDT
LAEFVRSNIR SVIEDSNVAD ILTPTEFPIC TKRACLDTNY YQTFNKPNVH IVDIKKDPIL
SISETGVTTR DQNFDFDAIV FATGFDAMTG ALLAIDIRGR DGQTLKEKWA DGPVNYLGLT
VSGFPNFFMI TGPGSPSVLS NMVLSIEQHV EWIADCLAYM EKEDLTVIDA TPMAETGWVE
YGTATSDMTL FPQAKSWYMG ANVPGKPRVC LPYVGGVAAY RRVCNDVAAQ DYLGFRFDGP
GGSRCKDGLV RRQQPDVVAL LEMLDEMELP PFESMSPEMA RATSLAMNAG NPPGPAVGEV
VDGQFPGADG LLDYRLYRPD SPGPHPVTVY FHGGGWVLGD HTSDDAFCRD LCVNANSIVI
SANYRHAPEA PFPAAADDGF AAVRWAAENI ETLGGIAGEL AVCGWSAGGN IAAVVCQLAR
DAGGPDIKGQ VLITPVVDAG DDSPSMTDNG EGFVLTKALM DWFWDHYADP SERADPKASP
LLAADLSHLP PALIITGEFD PLRDQGKAYA DALAAAGTQA RNITYPGQIH TSFTAVGAIP
TANGARQEVA AALRHYFKVM EPA
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