ID A0A0Q6XUT6_9BURK Unreviewed; 697 AA.
AC A0A0Q6XUT6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KQW03037.1};
GN ORFNames=ASC87_01500 {ECO:0000313|EMBL:KQW03037.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQW03037.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQW03037.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQW03037.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW03037.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQW03037.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQW03037.1}.
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DR EMBL; LMDI01000001; KQW03037.1; -; Genomic_DNA.
DR RefSeq; WP_056655477.1; NZ_LMDI01000001.1.
DR AlphaFoldDB; A0A0Q6XUT6; -.
DR STRING; 1736433.ASC87_01500; -.
DR OrthoDB; 5287258at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000051465; 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:UP000051465}.
FT DOMAIN 297..473
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 478..570
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 606..694
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 697 AA; 74557 MW; 168D51720C0B8988 CRC64;
MSATYEIRGP VAVITLTNPP VNGLGLSTRK GITDGIERAQ NDAAVKAVVI TGAGKAFSGG
ADIREFGSPL AYASPDLLSV IAAVEASSKP VVAAIQSVVM GGGLELALGC HYRVVAPGTQ
VALPEVKLGL LPGAGGTQRL PRVLGLETAL NLIASGDTAK SEQLAALPGQ KLFDQVADGD
VVAAAIAFAT NVADRRPLPR VRDLKVVHTD AEAYLQFARN TVGAMSKNFP APLQCVEAVA
ASINKPFDAG MQVEREIFSA LMLTPESRAQ RHMFFAERAA SKIPDVPADT PVRTIAKVGV
IGAGTMGGGI AMNFLNAGIP VTILETKQDA LDRGLATVRK NYEAQVKKGK LTQEKLDQRL
ALLSSTLAYD DLKDVDLVIE AVFEDINVKA QVFKALDEVC KPGAILASNT STLDVDKIAA
FTKRPQDVVG MHFFSPANVM KLLEVVRGAK TAKDVLATVM QLGKKIRKTC VVSGVCDGFI
GNRMIEQYSR QAGFLLDEGA SPQQVDKAVE KFGFAMGPFR MGDLAGNDIG WYIRKRRYIE
QPDMRYSKSA DLLCELGRYG QKTSAGWYDY VPGKRDAIPS PVVAEMLEKH RAALGIAPRR
ISDEEIVQRL VYALVNEGAK IVEEGIASKA SDIDMVYLAG YGFPLHRGGP MCYADTQGLF
NVVAAMKRFA KNPNDDASFW VPAPLLAKLA DEGKTFS
//
