ID J9SD32_9ACTN Unreviewed; 394 AA.
AC J9SD32;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=3-Hydroxy-9,10-seconandrosta-1,3,5(10)-trien-9, 17-dione (3-HSA) hydroxylase, oxygenase component {ECO:0000313|EMBL:AFR51376.1};
GN Name=hsaA {ECO:0000313|EMBL:AFR51376.1};
GN ORFNames=KTR9_0820 {ECO:0000313|EMBL:AFR51376.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR51376.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR51376.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR51376.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002907; AFR51376.1; -; Genomic_DNA.
DR RefSeq; WP_010842128.1; NC_018581.1.
DR AlphaFoldDB; J9SD32; -.
DR STRING; 337191.KTR9_0820; -.
DR KEGG; gor:KTR9_0820; -.
DR PATRIC; fig|337191.3.peg.1027; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_2_0_11; -.
DR Proteomes; UP000003281; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd01159; NcnH; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR InterPro; IPR013107; Acyl-CoA_DH_C.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR48083:SF19; FLAVIN-DEPENDENT MONOOXYGENASE, OXYGENASE SUBUNIT HSAA; 1.
DR PANTHER; PTHR48083; MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR PIRSF; PIRSF016578; HsaA; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}.
FT DOMAIN 22..103
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 240..372
FT /note="Acyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08028"
FT COILED 6..33
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 394 AA; 43434 MW; B4DC09F39B72CB83 CRC64;
MPAQRSEAAE QVLEKINVLL PELEQRAQST EDLRRIPDET VSSLETAGFF RLLQPEQWGG
YEADPVTFYE AVRRIASACG STGWVSGIIG VHNWHLALFD QQAQEDVWGS DTNVRISSSY
APMGMGEVVD GGYKVNGSWA WSSGCETADW VFVGGPVIKN GKPVDFVSFL IPREDYTIRD
VWNVVGLRGT GSNTIEVKDV FVPRHRMLSM RTMSMGQSPG LERNTAPVYK MPWGTIHPST
IATPIVGMAY GAYRAHVEHQ GKRVRAAYAG EKAKEDPFAK VRIAEAASDI DAAWRQLSGN
LQAEYDLILA GEEIPMELRL SARRDQVRAT GRAIAAIDRL FENSGAHALE NGTPIQRFWR
DAHAGRVHAA NDPERAYVAF GNGEFGIPIG DTMV
//
