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Database: UniProt
Entry: V7CA14_PHAVU
LinkDB: V7CA14_PHAVU
Original site: V7CA14_PHAVU 
ID   V7CA14_PHAVU            Unreviewed;       779 AA.
AC   V7CA14;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ESW26168.1};
GN   ORFNames=PHAVU_003G096400g {ECO:0000313|EMBL:ESW26168.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW26168.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA;
CC         Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316;
CC         EC=5.1.2.3; Evidence={ECO:0000256|ARBA:ARBA00023701};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097;
CC         EC=5.3.3.8; Evidence={ECO:0000256|ARBA:ARBA00000765};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00023709};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA;
CC         Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489;
CC         EC=5.3.3.8; Evidence={ECO:0000256|ARBA:ARBA00000452};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00023717};
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
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; CM002290; ESW26168.1; -; Genomic_DNA.
DR   RefSeq; XP_007154174.1; XM_007154112.1.
DR   AlphaFoldDB; V7CA14; -.
DR   STRING; 3885.V7CA14; -.
DR   EnsemblPlants; ESW26168; ESW26168; PHAVU_003G096400g.
DR   GeneID; 18634419; -.
DR   Gramene; ESW26168; ESW26168; PHAVU_003G096400g.
DR   KEGG; pvu:PHAVU_003G096400g; -.
DR   eggNOG; KOG1683; Eukaryota.
DR   OMA; ESTTIRW; -.
DR   OrthoDB; 622692at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000000226; Chromosome 3.
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:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004300; F:enoyl-CoA hydratase 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; IPR006180; 3-OHacyl-CoA_DH_CS.
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; 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.
DR   PROSITE; PS00067; 3HCDH; 1.
PE   3: Inferred from homology;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226}.
FT   DOMAIN          368..546
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          549..642
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   779 AA;  85257 MW;  E28E41BA92218225 CRC64;
     MELKGCGVER EWYDVIVFPI QQDIPFTTLP VISLNFSFGF KSNLNNRKPK ESHHSTMGRG
     GGHTRMEVGS DGVAVITIVN PPVNSLSFEV LHGLKESFDQ AIKRNDVKAI VVTGAKGKFS
     GGFDISAFGG IQEAKDRPKP GWISIEIITD TIEAARKPSV AAIDGLALGG GLEVAMACNA
     RLSTPTSQLG LPELQLGIIP GFGGTQRLPR LVGLTKALEM ILASKPVKGK EAFSLGLVDG
     LVQPNDLVNT ARQWALDILG RQRPWVASLY KTDKLESLGE AREILKFARA QAQRRAPNLY
     HPLVCIDVIE AGIVAGPRAG LWKEAEAFEK LVQSDICKSL VHVFFAQRGT TKVPGVTDRG
     LVPRQIKKVA ILGGGLMGSG IATALILSNY PIILKEVNGK FLDAGINRIK ANLQSRVKKG
     KMTKENFAKA VSLVSGSLDY ESFRDVDMVI EAVIENVSLK QQIFVDLEKY CPPHCILASN
     TSTIDLNLIG EKIKSKDRIV GAHFFSPAHV MPLLEIVRTK QTSSQVIVDV LNISKKIRKT
     PVVVGNCTGF AVNRMFFPYT QAGLLLVERG ADVYQIDRVI TKFGMPMGPF RLVDLVGFGV
     AIATGSQFIQ NFPERTYKSM LIPLLQEDKR AGETTRKGFY LYDDKRKASP DPELKNYIEK
     ARGISGVSVD PKLAKIPEKD IVEMIFFPVV NEACRVLDEG IAVKAADLDI SAIMGMGFPP
     YRGGIIFWAD SFGSKYIYSR LQKWSELYGE FFKPCAYLAA RAAKGIPLSA PVEQAKSRM
//
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