ID B5ZPJ9_RHILW Unreviewed; 737 AA.
AC B5ZPJ9;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase NAD-binding {ECO:0000313|EMBL:ACI53516.1};
GN OrderedLocusNames=Rleg2_0216 {ECO:0000313|EMBL:ACI53516.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI53516.1, ECO:0000313|Proteomes:UP000008330};
RN [1] {ECO:0000313|EMBL:ACI53516.1, ECO:0000313|Proteomes:UP000008330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304 {ECO:0000313|EMBL:ACI53516.1,
RC ECO:0000313|Proteomes:UP000008330};
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
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}.
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DR EMBL; CP001191; ACI53516.1; -; Genomic_DNA.
DR RefSeq; WP_012556536.1; NC_011369.1.
DR AlphaFoldDB; B5ZPJ9; -.
DR STRING; 395492.Rleg2_0216; -.
DR KEGG; rlt:Rleg2_0216; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR HOGENOM; CLU_009834_15_0_5; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000008330; Chromosome.
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 328..507
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 509..606
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 737 AA; 78812 MW; C3B6EE20E28E4801 CRC64;
MTYINFTLET DADGIALVTW DMPGKSMNVF TSEVMAELDA IIDATTADAA VKGVVFTSGK
SSFSGGADLS MIKSMFGSYQ DEKEKSPETA VQTLFGLVGR MSGLFRKLET SGKPWVSAIN
GTCMGGAFEL SLACHGRVAS NAKSVKIALP EVKVGIFPGA GGTQRVPRLA NAQDALQMMT
TGQSLSGSRA KAMNLVHQVV EPDQLIPAAK QMIKDGLKPV APWDEKGFKL PGGGIWTPAS
AQLWPAAPAI LRRETSGNYP AALAILKCVY EGLQLPFDTG LKIEQRYFTE VLQTREAFSM
IRSLFISMQE LGKGARRPAG IPKTELKHVG VVGAGFMGAS IAYVTAAAGL AVTLIDRDME
AAAKGKAVCE GLVKDSVGKG RFTQDEAAAL LARITPSANY ADLAAAGLVI EAVFEDREVK
KAVIEAVEAV LPEGAIFASN TSTLPISGLA KNSKRPADFI GIHFFSPVEK MMLTEVILGK
ATGDKALAVA LDYVAAIKKT PIVVNDTRGF FVNRCVLRYM SESYDMLIEG VPPTMIENAA
KMAGMPVGPL ALNDEVAIDL SLKILKATVA DLGEEAIDPR HMDLISRMVE KEGRFGRKNS
KGFYDYPPKP AKKSLWPELK TLYPQRRADE VDVNVLKQRF LVTIALEAAR TVEEGIVTDP
READVGSILG FGFAPYTGGA LSYIDGMGAK AFVELAEKLA GTYGDHFKPT PLLKDMAAKG
ETFYGRFDPY AGAKVAA
//
