ID A0A418Q2D9_9SPHN Unreviewed; 694 AA.
AC A0A418Q2D9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:RIX32017.1};
GN ORFNames=D3M59_03265 {ECO:0000313|EMBL:RIX32017.1};
OS Sphingomonas edaphi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2315689 {ECO:0000313|EMBL:RIX32017.1, ECO:0000313|Proteomes:UP000285023};
RN [1] {ECO:0000313|EMBL:RIX32017.1, ECO:0000313|Proteomes:UP000285023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAC4 {ECO:0000313|EMBL:RIX32017.1,
RC ECO:0000313|Proteomes:UP000285023};
RA Seo T.;
RT "Sphingomonas sp. DAC4.";
RL Submitted (SEP-2018) 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:RIX32017.1}.
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DR EMBL; QXTF01000001; RIX32017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418Q2D9; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000285023; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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 Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT DOMAIN 305..481
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 486..570
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 605..689
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 694 AA; 75563 MW; 1584E3F8C581AB03 CRC64;
MTDVIDTPTI NPISTSRHGD VMIVTSNNPP VNALGAAVRK GLVAAIEEAD GDEGVQAVVI
RCEGQTFFAG ADITEFGKPP VMPWLPTVVD TIENCSKPVV AAIHGTALGG GLEVALGCHY
RVAVKEAKLG VPEVKLGLLP GAGGTQRLPR VAGVQKALEM VTSGAMVSAR DACDVGLIDR
IVEGDLLQHA VAYAEEVRDV RPLPKSSERD EKLADARANP AIFDEFRKTN ARKFRGFEAP
EANIKAVEAA VAKPYAEGVI DERNLFMGLM SGVQSRAQQY FFFAERKAAK IEGIPDDTKP
RAINKVGVIG AGTMGGGISM NFLSAGIPVT VFELNQEALD RGTGVMRRNY EATASKGRMT
GEQVERAMDL LTPTLEFDAL AGCDLIIEAV FEQMEVKKEI FTRLDKVMKP GAILASNTSY
LNIDEIAAVT SRPQDVVGLH FFSPANIMKL LEVVRGAKTA PDVLVTAMQL AKKIKKVAVV
AGVCHGFIGN RMLMPRQVEA TKLLLEGATP EQIDRVHVEF GMPMGPFQMA DLAGVDIGWH
RDPTRIENIR DALAAEGRWG QKKQAGFYDY DDKRRPSPSP RVQEIIDDFA AKQGVTRRDI
SDEEIIQRTL YTMVNEGAKI LEEGMAQRAS DIDVVWVYGY GWPVYRGGPM FWADTEGLQK
IVDGLRAQRD QMGSDFSFSQ LLLDKAEKGE KFTR
//
