HSAA_RHOJR
ID HSAA_RHOJR Reviewed; 382 AA.
AC Q0S811;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Flavin-dependent monooxygenase, oxygenase subunit HsaA;
DE EC=1.14.14.12;
DE AltName: Full=3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4-hydroxylase, oxygenase subunit;
DE AltName: Full=3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase;
GN Name=hsaA; OrderedLocusNames=RHA1_ro04539;
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=101510;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1;
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
RN [2]
RP FUNCTION IN CHOLESTEROL DEGRADATION.
RC STRAIN=RHA1;
RX PubMed=17264217; DOI=10.1073/pnas.0605728104;
RA Van der Geize R., Yam K., Heuser T., Wilbrink M.H., Hara H., Anderton M.C.,
RA Sim E., Dijkhuizen L., Davies J.E., Mohn W.W., Eltis L.D.;
RT "A gene cluster encoding cholesterol catabolism in a soil actinomycete
RT provides insight into Mycobacterium tuberculosis survival in macrophages.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1947-1952(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND SUBUNIT.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of 3-hsa hydroxylase, oxygenase from Rhodococcus sp.
RT RHA1.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the o-hydroxylation of 3-hydroxy-9,10-secoandrosta-
CC 1,3,5(10)-triene-9,17-dione (3-HSA) to 3,4-dihydroxy-9,10-secoandrosta-
CC 1,3,5(10)-triene-9,17-dione (3,4-DHSA) in the catabolism of
CC cholesterol. {ECO:0000269|PubMed:17264217}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione +
CC FMNH2 + O2 = 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-
CC dione + FMN + H(+) + H2O; Xref=Rhea:RHEA:31731, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15896,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63245;
CC EC=1.14.14.12;
CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis.
CC -!- SUBUNIT: Homotetramer. HsaAB monooxygenase consists of an oxygenase
CC component HsaA and a reductase component HsaB. {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the HpaH/HsaA monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; CP000431; ABG96325.1; -; Genomic_DNA.
DR PDB; 2RFQ; X-ray; 1.65 A; A/B/C/D=1-382.
DR PDBsum; 2RFQ; -.
DR AlphaFoldDB; Q0S811; -.
DR SMR; Q0S811; -.
DR STRING; 101510.RHA1_ro04539; -.
DR EnsemblBacteria; ABG96325; ABG96325; RHA1_ro04539.
DR KEGG; rha:RHA1_ro04539; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_2_0_11; -.
DR OMA; DVWHVVG; -.
DR BioCyc; MetaCyc:MON-16961; -.
DR UniPathway; UPA00062; -.
DR EvolutionaryTrace; Q0S811; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0036383; F:3-hydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione monooxygenase activity; IEA:UniProtKB-EC.
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 GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 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.
DR Pfam; PF08028; Acyl-CoA_dh_2; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Flavoprotein; FMN;
KW Lipid degradation; Lipid metabolism; Monooxygenase; Oxidoreductase;
KW Reference proteome; Steroid metabolism.
FT CHAIN 1..382
FT /note="Flavin-dependent monooxygenase, oxygenase subunit
FT HsaA"
FT /id="PRO_0000404502"
FT BINDING 72
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 106..108
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 129..131
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 334..335
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 356..357
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT HELIX 1..13
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:2RFQ"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:2RFQ"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:2RFQ"
FT STRAND 120..130
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2RFQ"
FT STRAND 137..147
FT /evidence="ECO:0007829|PDB:2RFQ"
FT STRAND 150..160
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2RFQ"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2RFQ"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2RFQ"
FT STRAND 181..191
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:2RFQ"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 221..254
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 265..297
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 304..332
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 342..353
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:2RFQ"
FT HELIX 361..372
FT /evidence="ECO:0007829|PDB:2RFQ"
SQ SEQUENCE 382 AA; 41868 MW; 18FA78081331E1AB CRC64;
MQRLDALLPT LRERAQETED LRRIPDDSMK ALQETGFFRL LQPEQWGGYQ ADPVLFYSAV
RKIASACGST GWVSSIIGVH NWHLALFSQQ AQEDVWGNDT DVRISSSYAP MGAGQVVDGG
YTVNGAWAWS SGCDHASWAV LGGPVIKDGR PVDFVSFLIP REDYRIDDVW NVVGLRGTGS
NTVVVEDVFV PTHRVLSFKA MSNLTAPGLE RNTAPVYKMP WGTIHPTTIS APIVGMAYGA
YDAHVEHQGK RVRAAFAGEK AKDDPFAKVR IAEASSDIDA AWRQLSGNVA DEYALLVAGE
EVPFELRLRA RRDQVRATGR AISSIDKLFE SSGATALANG TPLQRFWRDA HAGRVHAAND
PERAYVMYGT GEFGLPITDT MV
