ID A0A2E7P2R2_9BURK Unreviewed; 709 AA.
AC A0A2E7P2R2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:MBO16021.1};
DE Flags: Fragment;
GN ORFNames=CME87_11115 {ECO:0000313|EMBL:MBO16021.1};
OS Herbaspirillum sp.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1890675 {ECO:0000313|EMBL:MBO16021.1, ECO:0000313|Proteomes:UP000226028};
RN [1] {ECO:0000313|Proteomes:UP000226028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Graham E.D., Heidelberg J.F.;
RT "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT Global Oceans.";
RL Submitted (SEP-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:MBO16021.1}.
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DR EMBL; PBPP01000071; MBO16021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2E7P2R2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000226028; 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 Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT DOMAIN 309..485
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 490..583
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 621..703
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT NON_TER 709
FT /evidence="ECO:0000313|EMBL:MBO16021.1"
SQ SEQUENCE 709 AA; 75802 MW; 4C0EF567BCA9A8A1 CRC64;
MSKQSTAAGE TPPVHLAREG AILVVTIDNP PVNALGVAVR RGLMSAIEEG EADAGVAAIL
VTGAGRNFIG GADIREFGKP PQSPLLTELC NRIEVCSKPV LAAIHGAALG GGLEVALAAH
YRVALSNARL GLPEVQLGLL PGAGGTQRTP RLIGAQAALD MMLSGRHLSA KEALSLGLVD
QLAEGDSADQ ARAAGLRELQ ALLDTHAPVR RSRDGKGLAD TAATQAAIAA ARDEAGKKSR
GLFSPHKIID AVEAATNLTF EEGLALERQF FLQCLDSPQR AGLIHAFFAE REVQKAPETR
NAQPRRIEQI GVVGGGTMGA GIAVAVLDAG LPVTMIERDD EALARGRGHV EKVYDAQVTK
GRLTQEARDA VLARLQGSTR YEDLSAADVV IEAVFEDLTV KQAVFAELDR VCKPGAVLAT
NTSYLDIDAI AASISRPADV IGLHFFSPAN VMKLLEIVVP RQVAADVVAT AFELAKRLRK
VPVRAGVCDG FIGNRILAVY RQAADALMED GASPYEIDAA VRDFGFAMGP YQVVDLAGGD
IGWATRKRRA ATRDPRARYV HIADRLCERG WFGQKSGRGF YRYPDGPRSG APDPEVLALI
DEERARAGIT PRSFSKEDIQ RRYLAAMINE GANVVHQRIA LRPLDVDVTF LYGYGFPRHR
GGPMKYADMV GLPNVLADIR AFAAEDPLFW TPSPLLVELV ERGANFESL
//