ID A0A0U1Q0B0_9BURK Unreviewed; 699 AA.
AC A0A0U1Q0B0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KKW68171.1};
GN ORFNames=AAV94_06850 {ECO:0000313|EMBL:KKW68171.1};
OS Lampropedia cohaerens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Lampropedia.
OX NCBI_TaxID=1610491 {ECO:0000313|EMBL:KKW68171.1, ECO:0000313|Proteomes:UP000050580};
RN [1] {ECO:0000313|EMBL:KKW68171.1, ECO:0000313|Proteomes:UP000050580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT6 {ECO:0000313|EMBL:KKW68171.1,
RC ECO:0000313|Proteomes:UP000050580};
RA Tripathi C., Rani P., Mahato N.K., Lal R.;
RT "Draft genome sequence of Lampropedia sp. CT6, isolated from the microbial
RT mat of a hot water spring, located at Manikaran, India.";
RL Submitted (MAY-2015) 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 -!- 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:KKW68171.1}.
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DR EMBL; LBNQ01000022; KKW68171.1; -; Genomic_DNA.
DR RefSeq; WP_046741570.1; NZ_LBNQ01000022.1.
DR AlphaFoldDB; A0A0U1Q0B0; -.
DR STRING; 1610491.AAV94_06850; -.
DR PATRIC; fig|1610491.3.peg.1452; -.
DR OrthoDB; 5287258at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000050580; 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; 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.
PE 4: Predicted;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050580}.
FT DOMAIN 299..475
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 480..572
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 608..696
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 699 AA; 75984 MW; 5406FCFBB9C9855E CRC64;
MTAEYKVHDG VAVITLNNPP VNGLGYATRK AIVSGIEQAN ADDTVSAIVI TGAGKAFSGG
ADITEFGKDI AFREPNLHGV IEIVENSPKP VVAAMHSVVM GGGLELALAC HYRVVAAGTK
VALPEVKLGL LPGAGGTQRL PRVIGVEAAL NMIVSGETVD AQLLASLPGQ KLFDEVVDDP
ASLADEALAF ARSVARVTDL PRVRDLPAKH PQGEAFFQFA RNTAGAVAKN LPAPIKCVDA
VEAATTLPFA QGLARERELF IQLMGTPESR ALRHFFFAER AASKIDDVPP DTPQREIRKV
GIIGAGTMGG GIAMNFLNAG FPVVILETKQ EALERGVGVI RKNYEDRIKK GKLKQEKYEQ
TIALLSTTLD YQDLQDVDLV IEAVFEDIGV KEQVFRKLDE VVKPGAILAS NTSTLDLNRI
ASFTQRPQDV VGMHFFSPAN VMKLLEVVRG AQTAKDVLAT VMALAKKIRK VAVVAGVTDG
FIGNRMIEQY ARQAGFLLDE GATPQQVDKA IENFGFAMGP FRMGDLAGND IGWAIRKRRA
VEQPDLRYSR TADLLCEKGR FGQKTGAGWY DYAPGKRDPI VSQEVLDMIE QHRKDAGITP
RRISDEEIVQ RLVFSLVNEG ARIVEEGFAQ RASDIDVVYI YGYGFPFWRG GPMHYANEVG
LFSVIEAMKR FARNPLDDAA FWQPASLLRQ LAAEGKQFQ
//
