ID K4Q6C9_9RHOO Unreviewed; 287 AA.
AC K4Q6C9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:CCH23024.1};
OS Azoarcus sp. CIB.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=198107 {ECO:0000313|EMBL:CCH23024.1};
RN [1] {ECO:0000313|EMBL:CCH23024.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CIB {ECO:0000313|EMBL:CCH23024.1};
RX PubMed=22759228; DOI=10.1111/j.1462-2920.2012.02818.x;
RA Juarez J.F., Zamarro M.T., Eberlein C., Boll M., Carmona M., Diaz E.;
RT "Characterization of the mbd cluster encoding the anaerobic 3-
RT methylbenzoyl-CoA central pathway.";
RL Environ. Microbiol. 15:148-166(2013).
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC {ECO:0000256|ARBA:ARBA00005086}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009463}.
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DR EMBL; HE801912; CCH23024.1; -; Genomic_DNA.
DR RefSeq; WP_050417918.1; NZ_CP011072.1.
DR AlphaFoldDB; K4Q6C9; -.
DR STRING; 198107.AzCIB_4486; -.
DR PATRIC; fig|198107.6.peg.4639; -.
DR OrthoDB; 5287258at2; -.
DR GO; GO:0008691; F:3-hydroxybutyryl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
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; IPR013328; 6PGD_dom2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR48075:SF5; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR PIRSF; PIRSF000105; HCDH; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00067; 3HCDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000105-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 3..181
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 185..281
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT BINDING 8..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 90
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT BINDING 273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-2"
FT SITE 138
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 287 AA; 31568 MW; 96564EF64F18F8FF CRC64;
MEKIAVIGAG AMGRQIALQC ALSGLKTVLN DSRKESLEQA ADFVREHLDK RVAKGRISSE
QRATALGNLD LAPDLAAAAD ADLIIEAIVE KFEPKAELFR TLDRLCPPQT IFGTNSSNIR
GSRLAGVTAR PQRVLNIHFF NPALVMELVE VVVHPAVPAE IIEEVLAFCR SIGKTPVVLR
KEIPGFIVNR IFRALTREAV SLYEEGYASA EDIDLAVTKG LGHPMGPLRL LDTTGIDVSY
LARMDEYEET SVESAKPNRL LKEMYERGEW GKKSGKGFYI YGDDKAK
//
