ID T0IFE7_9SPHN Unreviewed; 731 AA.
AC T0IFE7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:EQB08339.1};
GN ORFNames=L288_08290 {ECO:0000313|EMBL:EQB08339.1};
OS Sphingobium quisquiliarum P25.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1329909 {ECO:0000313|EMBL:EQB08339.1, ECO:0000313|Proteomes:UP000015525};
RN [1] {ECO:0000313|EMBL:EQB08339.1, ECO:0000313|Proteomes:UP000015525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P25 {ECO:0000313|EMBL:EQB08339.1,
RC ECO:0000313|Proteomes:UP000015525};
RX PubMed=24029763;
RA Kumar Singh A., Sangwan N., Sharma A., Gupta V., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium quisquiliarum Strain P25T, a Novel
RT Hexachlorocyclohexane (HCH)-Degrading Bacterium Isolated from an HCH
RT Dumpsite.";
RL Genome Announc. 1:e00717-13(2013).
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}.
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:EQB08339.1}.
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DR EMBL; ATHO01000070; EQB08339.1; -; Genomic_DNA.
DR AlphaFoldDB; T0IFE7; -.
DR PATRIC; fig|1329909.3.peg.1600; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000015525; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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 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}.
FT DOMAIN 331..507
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 510..606
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 731 AA; 77869 MW; CEFA0E3689FDFA0C CRC64;
MRGSIIMQTI AFDVDADGIA TLTIDVPGQS MNVIGPEFLA DLDEAVTRIA SDEAVKGAVI
ASGKEAGFMA GLDLKYFGSM LASESGKRPA PAEIFDKVFI LNRLLRRLET CGKPVACAIE
GTCVGGGFEL ALACHHRVAG DSSRTQMGLP EILIGLFPGG GGSQRLPRII GVQAALLYML
QGKLFRPAEA AMMKVVDEVV PQGTAVAAAI QWVKANPSAS VQPWDQKGFK FPGGAGGFNP
AFVQTMAGAL PMTLKQTQRN MNAPIALLSA VYEGAILPFD RAIRIESKYF AKVAADPQAA
NMIRSLFVNK QAAERGARRP ADQPKAPTRK LAMLGAGMMG AGIATVAAQA GMEVILFDRD
LSFAEKGKAH VEEQLKKRLG KGMTPEKMAE TLARVTPATD YAALAGADFV IEAVFEDAAI
KAEVTKKVEA VLGPDVIFGS NTSTLPITKL AGAWSKPANF IGIHFFSPVE KMPLVEIILG
KETGPAAIAK AMDFVAQIKK TPIVVNDSRG FYTSRCFGTY VQEGVEMVAE GINPALIENA
GRQLGMPVGP LAVGDEVSIE LGHKVVLAAQ KDLGDAYVAQ PSDAVTARMV ELGRLGRKSG
KGWYDYPEGG KKHLWTGLEE MFPRAPVQPD VEEVKERLLY RQLVECARCY EEGVLETPED
GDIGAIFGWG FAAWTGGPFS HMDTLGIGPV VAVLERLAAR HGERFAPTVQ LQDMAASGAT
FYDAERVRAA A
//
