ID J1RVY9_9ACTN Unreviewed; 734 AA.
AC J1RVY9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Enoyl-CoA hydratase/isomerase family protein {ECO:0000313|EMBL:QTZ95035.1};
DE SubName: Full=NAD-binding protein 3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:EJJ08704.1};
GN ORFNames=SU9_02282 {ECO:0000313|EMBL:EJJ08704.1}, SU9_029255
GN {ECO:0000313|EMBL:QTZ95035.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ08704.1};
RN [1] {ECO:0000313|EMBL:EJJ08704.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ08704.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ95035.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ95035.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00023693};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR EMBL; AJGV01000018; EJJ08704.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ95035.1; -; Genomic_DNA.
DR RefSeq; WP_006602043.1; NZ_CP072931.1.
DR AlphaFoldDB; J1RVY9; -.
DR STRING; 1160718.SU9_02282; -.
DR KEGG; sauh:SU9_029255; -.
DR PATRIC; fig|1160718.3.peg.473; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_16_0_11; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000009036; Chromosome.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 1.10.1040.50; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isomerase {ECO:0000313|EMBL:QTZ95035.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000009036}.
FT DOMAIN 325..503
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 506..606
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 734 AA; 78648 MW; 6FACCDACB98CA8E3 CRC64;
MSESPASSTI RWEQDETGIV TLVLDDPDQS ANTMNNAFKA SLTAVADRLE AEKDSIRGII
FTSAKKTFFA GGDLRELIAI TPAQAQQAFE TGNGIKRDLR RIETLGKPVV AAINGAALGG
GYEIALACHH RIALDTPGTK IGLPEVTLGL LPAGGGVTRT VRLLGITDAL LKVLLQGTQY
NAGRAKDAGL IHEVAATPEE LLAKARAFVD EHPESQQPWD VKGYRIPGGT PAQPKFAANL
PAFPANLKKQ LNGAPYPAPR NILAAAVEGS QVDFETAQTI EARYFVELVT GQISKNMIQA
FFFDLQAVNS GANRPKDIEP RKVEKVAVLG AGMMGAGIAY SCAKAGMQVV LKDLSLEAAQ
KGKAYTEGLL AKALSRGRTT EQQRDELLAR ITPTAEPADL AGCDAVIEAV FEDVGLKHKV
FKEIQHIVAP DALLCSNTST LPITLLAEGV EREQDFIGLH FFSPVDKMPL VEIIKGERTG
DEALARAFDL VRQIRKTPIV VNDSRGFFTS RVIGHFINEG VAMIGEGLDP VSVEQAAAQA
GYPAKVLSLM DELTLTLPRK IREESKRAVE ESGGTWQPHP ADAVIDRMVD EFGRPGRSGG
AGFYEYGDDG KRAGLWPGLR EHFAQEGAAI PFADMQERML FSEALDTVRC LEEGVLTSVA
DANIGSILGI GFPGWTGGVL QYINGYQGGP GREELVGLPG FVARARELQA AYGDRFAPSP
LLVEKAGKGE KFSD
//