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Database: UniProt
Entry: A0A0E3ULG0_9GAMM
LinkDB: A0A0E3ULG0_9GAMM
Original site: A0A0E3ULG0_9GAMM 
ID   A0A0E3ULG0_9GAMM        Unreviewed;       790 AA.
AC   A0A0E3ULG0;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:AKC85446.1};
GN   ORFNames=WQ53_00300 {ECO:0000313|EMBL:AKC85446.1};
OS   Pseudoxanthomonas suwonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=314722 {ECO:0000313|EMBL:AKC85446.1, ECO:0000313|Proteomes:UP000033067};
RN   [1] {ECO:0000313|EMBL:AKC85446.1, ECO:0000313|Proteomes:UP000033067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J1 {ECO:0000313|EMBL:AKC85446.1,
RC   ECO:0000313|Proteomes:UP000033067};
RX   PubMed=26067962;
RA   Hou L., Jiang J., Xu Z., Zhou Y., Leung F.C.;
RT   "Complete Genome Sequence of Pseudoxanthomonas suwonensis Strain J1, a
RT   Cellulose-Degrading Bacterium Isolated from Leaf- and Wood-Enriched Soil.";
RL   Genome Announc. 3:e00614-15(2015).
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}.
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DR   EMBL; CP011144; AKC85446.1; -; Genomic_DNA.
DR   RefSeq; WP_052629484.1; NZ_CP011144.1.
DR   AlphaFoldDB; A0A0E3ULG0; -.
DR   KEGG; psuw:WQ53_00300; -.
DR   PATRIC; fig|314722.6.peg.65; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   OrthoDB; 5389341at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000033067; Chromosome.
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; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF7; 3-HYDROXYACYL-COA DEHYDROGENASE-RELATED; 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   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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033067}.
FT   DOMAIN          10..192
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          195..293
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   790 AA;  85652 MW;  7E1FB1859A7DBA4B CRC64;
     MSEKLLVRRA AVLGAGVMGA QIAAHLTNAG VDTVLFDLAA KEGPADGVVL KALAHLGKLS
     PAPLAGKSLA EAITPANYDT GLEQLKDCDL IIEAIAERMD WKQDLYRKIA PFVADHAVLA
     SNTSGLGVNR LAEVLPEQLR HRFCGVHFFN PPRYMHLAEL IPARTTDKAV LEGLETFLTT
     QLGKGVVYAK DTPNFIGNRI GVFSILSVIH HTRQFGLGFD EVDALTGPLV GRPKSATYRT
     SDVVGLDTMA HVIKTMADTL PNDPWHSYFQ SPDWLAALVG KGALGQKAGA GIFRKVGKDI
     VVLDLEKQDY RAADRKAADE VVEILKIRNP AEKFARLRES AHPQAQFLWA AFRDLFHYSA
     YHLADIAQTA RDVDLAIRWG YGWSLGPFET WQAAGWKQVA QWIADDIAAG KTMSDAPLPA
     WVLDGRDDVH AAEGSYSPAQ DALVPRSSLP VYRRQRFPDP LLGERFDPGQ TVFENDGVRL
     WHDGDGIAVV SFKTKMNTVS DQVLDGLQEA IAIAERDFQG LVIWQQKEPF SAGADLAGAL
     GLLQAGKVDA FEAMVANFQR TSQRIKYALV PVVAAVRGLA LGGGCEFQMH AARTVAHLES
     YIGLVEAGVG LLPAGGGLKE LAVRASRAAG PGGDVFAELK KTFEAVAMAK VSASALEAKE
     LGLLRADDTI VFNAFELLHV AKAQARALAE AGYRPPLPAR RVQVAGDVGV ATFRMLLVNM
     LEGRFISPYD DEIATRIATV LCGGEVDRGA LVDEEWLIGL ERKHFVELAQ QEKTQARIGH
     MLKTGKPLRN
//
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