ID A0A2G2Z6J0_CAPAN Unreviewed; 754 AA.
AC A0A2G2Z6J0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a {ECO:0000313|EMBL:PHT77618.1};
GN ORFNames=T459_15670 {ECO:0000313|EMBL:PHT77618.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072 {ECO:0000313|EMBL:PHT77618.1, ECO:0000313|Proteomes:UP000222542};
RN [1] {ECO:0000313|EMBL:PHT77618.1, ECO:0000313|Proteomes:UP000222542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334 {ECO:0000313|Proteomes:UP000222542};
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
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: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
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:PHT77618.1}.
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DR EMBL; AYRZ02000006; PHT77618.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G2Z6J0; -.
DR STRING; 4072.A0A2G2Z6J0; -.
DR EnsemblPlants; PHT77618; PHT77618; T459_15670.
DR Gramene; PHT77618; PHT77618; T459_15670.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000222542; Chromosome 6.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
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:SF43; 3-HYDROXYBUTYRYL-COA EPIMERASE; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 2.
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; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Membrane {ECO:0000256|SAM:Phobius}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Plastid {ECO:0000256|ARBA:ARBA00022528};
KW Reference proteome {ECO:0000313|Proteomes:UP000222542};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 334..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 333..512
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 514..607
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 754 AA; 83854 MW; E791776C24D7B9F2 CRC64;
MEKQQRTKAC KNIELEVVEN GVAVISINHP PLNLLSVEVL LSLKENIEEA MRKDNVKAIV
ITGSRGNFSA GFDVTAFGGS QRRKTRKELG FMSIEFITDT FEAARKPIVA AVEGLALGGG
FEIALACHAR ISTSSAKLGL PELQYGILPG FGGGHGFKPW KQPLAEMQGT QRLPRLVGLP
KALEMILTSK RVSGEEACSM GLVDAMSPSD RLLGSACRWA LDILECRRPW SISLSRTDRL
APLAEARTLL NSARARMRKQ NPNVIHPLVC IDVIEHGILC GPRNGLWKEA EALHELRQSD
SCRSLVHVFF AKQRTSKIPG ITDTGLLPRK IRKVAILGGS LMSSGIATAL VFANHYVIMK
YMDQKSLENG IDGVKADLEG RLKEGKMTRE HYEKACALLR GVLSYDTFKD VDLVIEDMLD
VVSLKQQIFA DLDECCPPRC IFASTTCIVD LDLLGERMKT CREIVGVHFF SPPTATDLLE
IVRTERTSPQ VVVDLLNFGR RIRKTPIVVQ DCTGFAVRRM CFPYLQAAMF LVQHGADVYQ
IDKALTSFGM KLGPFRMLDR DGFQSAAVCD VKFLETFQDR SYESNLIPIM RKNNREGEST
RQGFYTYNDK GEASPDPEIS KYIEMTRNFI NDPNCSWKTY NAFNIYNLAT LSDGEIVEMI
LFAVLNEACL MISDAVIVKS SDLDVASVLG MGFPEYRGGI IFWSQSVGSE YICSKLEEWS
KEYGESFKPC AYLIERASKR CSLGAESKQA KSLL
//
