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Database: UniProt
Entry: A0A0A0MAH7_9GAMM
LinkDB: A0A0A0MAH7_9GAMM
Original site: A0A0A0MAH7_9GAMM 
ID   A0A0A0MAH7_9GAMM        Unreviewed;       791 AA.
AC   A0A0A0MAH7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KGO99359.1};
GN   ORFNames=N791_09115 {ECO:0000313|EMBL:KGO99359.1};
OS   Lysobacter defluvii IMMIB APB-9 = DSM 18482.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1385515 {ECO:0000313|EMBL:KGO99359.1, ECO:0000313|Proteomes:UP000030003};
RN   [1] {ECO:0000313|EMBL:KGO99359.1, ECO:0000313|Proteomes:UP000030003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMMIB APB-9 {ECO:0000313|EMBL:KGO99359.1,
RC   ECO:0000313|Proteomes:UP000030003};
RA   Wang Q., Wang G.;
RT   "Genomic analysis of Lysobacter defluvii.";
RL   Submitted (AUG-2013) 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:KGO99359.1}.
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DR   EMBL; AVBH01000020; KGO99359.1; -; Genomic_DNA.
DR   RefSeq; WP_027068919.1; NZ_AVBH01000020.1.
DR   AlphaFoldDB; A0A0A0MAH7; -.
DR   STRING; 1385515.GCA_000423325_00365; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   OrthoDB; 5389341at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000030003; Unassembled WGS sequence.
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:UP000030003}.
FT   DOMAIN          10..191
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          195..294
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   791 AA;  85663 MW;  E9CFD97EF8E64E58 CRC64;
     MSEKLLVRRA AVLGAGVMGA QIAAHLVNAG VDTVLFDLPA KEGKPNGVVE QAIARLGKLK
     PAPLAEKSLA ARITPANYET GLELLEGCDL VIEAIAERMD WKQDLYRKIA PHVPAHAVLA
     SNTSGLGINK LAEVLPGEMR PRFCGVHFFN PPRYMHLAEL IPARSTDDAV MQGLEAFLTT
     TLGKGVVYAR DTPNFIGNRI GVFSMLAAMH HTTQFGLGFD TVDALTGPAI GRPKSATYRT
     ADVVGLDTMA HVIKTMADTL PEDPWHKYFK APKWLSGLVE KGALGSKSGA GFYTKKGKDI
     LVLDLEAQDY RASDQSLDPE VAALLKEREP AKKFAALRAS GHPQAKFLWA CFRDTFHYSA
     YHLKDIAETA RDVDLAMRWG YGWSVGPFET WQAAGWKQVA DWIAEDIVAG EAMSNAELPD
     WVFDGREGVH SGAGSYSPAR DAMVPRSSNP VYARQRFPDA LLGEKASQGR TVFENDGVRM
     WADEGDDIAV VGFKTKMHTV NDHVLDGLQE AIRIAERDFR GLVVWQPKEP FSAGADLAGA
     LGLLQAGDVE GFDAMVANFQ RTSMAIKYSQ VPVVVAVRGL ALGGGCEFQM HAARTVLGLE
     SYIGLVEAGV GLLPAGGGLK ELAVRASERA GTGGDVFAEL KNVFETVAMA KVSTSALEAK
     SLGLARPEDV VVFNAFELLH VAKAQARALA ESGYRPPLPA RAIRVAGDVG IATFRMMLVN
     MLEGRFISEH DHEIATRIAT VLCGGEVDRG AVVDEEWLLR LEREHFVALA QMPKTQERIA
     HMLKTGKPLR N
//
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