ID A0A2A5W952_9GAMM Unreviewed; 704 AA.
AC A0A2A5W952;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:PDH32891.1};
GN ORFNames=CNF02_10440 {ECO:0000313|EMBL:PDH32891.1};
OS OM182 bacterium MED-G28.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; OMG group; OM182 clade.
OX NCBI_TaxID=1986256 {ECO:0000313|EMBL:PDH32891.1, ECO:0000313|Proteomes:UP000219329};
RN [1] {ECO:0000313|EMBL:PDH32891.1, ECO:0000313|Proteomes:UP000219329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED-G28 {ECO:0000313|EMBL:PDH32891.1};
RA Haro-Moreno J.M., Lopez-Perez M., De La Torre J., Picazo A., Camacho A.,
RA Rodriguez-Valera F.;
RT "Fine stratification of microbial communities through a metagenomic profile
RT of the photic zone.";
RL Submitted (AUG-2017) 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: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PDH32891.1}.
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DR EMBL; NTJZ01000012; PDH32891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5W952; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000219329; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR PANTHER; PTHR23309:SF9; PEROXISOMAL BIFUNCTIONAL ENZYME; 1.
DR Pfam; PF00725; 3HCDH; 2.
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.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT DOMAIN 297..469
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 477..569
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 605..691
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 704 AA; 75981 MW; E3FB54C49F71146B CRC64;
MSQVVSYELQ ANIGIITVNN PPVNALAQVV REGILNAVNT AQKDASEAII LCCDGRTFIA
GADITEFGKP PKEPGLPDVL TAIENSTKPI VAAIHGTALG GGFEVTLACH YRCAVASAKV
GLPEVKLGLL PGAGGTQRVP RIAGVQAALD MITSGNPVPA QKAKDMGLVD EVVEGEELLA
GAISYTKHLI ESGAPLKRIR DITIDSSTIE AGFFESARER LAKRARGQIA QDRIVSCLQA
AVELPIDEGL IRERELFKEL VNSPESAAMR HIFFAERQAA KIKDLAKDTA LRPIKSVAIL
GGGTMGGGIA MCFANVGIPV ILVEINDEAL ERGLSIVRKN YAITVQKGKL PADKMEQRIG
LISGTTDYGD ISDVDLVIEA VFENLDLKKE IFAKLDAACK PGAILATNTS YQDVDAIAEA
TARPEDVVGM HFFSPANVMK LLEVVRGEKT ADDVLATVMQ IGKKIGKVCA LSRVCYGFIG
NRMLGGYGRE AQMLLLDGCT PAQVDGALEG FGMAMGPLAM SDLAGLDVGY KARQGRTDLP
DDPKLYRMGT MLVEMGRYGQ KTGSGFYQYD PETRRRMSDP EVEALIKEEA DKLNVEQAHI
SDDEILARCF YPLINEGAKI LEEGIAQRAS DIDVVYIYGY AFPVAKGGPM HYADSVGLKN
VHEKICEFRD KYGEQYWNPS PLLKQLAEEG KTFAQWDKER SAPQ
//
