ID A0A445EKD7_ARAHY Unreviewed; 939 AA.
AC A0A445EKD7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=very-long-chain 3-oxoacyl-CoA synthase {ECO:0000256|ARBA:ARBA00012307};
DE EC=2.3.1.199 {ECO:0000256|ARBA:ARBA00012307};
GN ORFNames=Ahy_A01g000401 {ECO:0000313|EMBL:RYR75822.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR75822.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR75822.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR75822.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000256|ARBA:ARBA00001906};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the malic enzymes family.
CC {ECO:0000256|ARBA:ARBA00008785}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000256|ARBA:ARBA00005531}.
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:RYR75822.1}.
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DR EMBL; SDMP01000001; RYR75822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445EKD7; -.
DR STRING; 3818.A0A445EKD7; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000289738; Chromosome a01.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009922; F:fatty acid elongase activity; IEA:UniProtKB-EC.
DR GO; GO:0004470; F:malic enzyme activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006108; P:malate metabolic process; IEA:UniProt.
DR CDD; cd00831; CHS_like; 1.
DR Gene3D; 1.20.1370.30; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.10380; Malic enzyme, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR012392; 3-ktacl-CoA_syn.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR013601; FAE1_typ3_polyketide_synth.
DR InterPro; IPR012301; Malic_N_dom.
DR InterPro; IPR037062; Malic_N_dom_sf.
DR InterPro; IPR012302; Malic_NAD-bd.
DR InterPro; IPR001891; Malic_OxRdtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR31561; 3-KETOACYL-COA SYNTHASE; 1.
DR PANTHER; PTHR31561:SF103; 3-KETOACYL-COA SYNTHASE 11; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR Pfam; PF08392; FAE1_CUT1_RppA; 1.
DR Pfam; PF00390; malic; 1.
DR Pfam; PF03949; Malic_M; 1.
DR PRINTS; PR00072; MALOXRDTASE.
DR SMART; SM01274; malic; 1.
DR SMART; SM00919; Malic_M; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 622..747
FT /note="Malic enzyme N-terminal"
FT /evidence="ECO:0000259|SMART:SM01274"
FT DOMAIN 746..939
FT /note="Malic enzyme NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00919"
SQ SEQUENCE 939 AA; 103982 MW; A1DC558B3065F74C CRC64;
MADAKADAPL VPSSSRNLPD FKKSVRLKYV KLGYHYLISH GMYLFLSPLV VLISAQLSTF
SLQDLHDLWQ HLQYNLISVI LCSTLLVFLS TLYFLTRPRP VYLVNFACYK PEESRKCTKR
VFMEHSRLAG TFTEENLAFQ QKILERSGLG ENTYLPEAVL NIPPNPTMKE ARKEAETVMF
GAIDELFAKT SVNPKDIGIL IVNCSLFNPT PSLSAMVVNH YKLRGNIRSY NLGGMGCSAG
LISIDLAKDL LQAHPNSYAL IISMENITLN WYFGNDRSKL VSNCLFRMGG AAVLLSNKSS
DRRRSKYRLV TTVRTNKGAD DKCFSCVTQE EDEAGKIGVT LSKDLMAVAG DALKTNITTL
GPLVLPMSEQ LLFFATLVGK KLLKMKIKPY IPDFKLAFEH FCIHAGGRAV LDELEKNLQL
SPWHMEPSRM TLYRFGNTSS SSLWYELAYT EAKGRIRKGD RTWQIAFGSG FKCNSAVWKA
LKTINPAKEK NPWMDEIHKF PVEVPRRCGT WHDLAPPPLP DRGGRSRRRF PGLSLFTSAV
LISSTILGST RLLQTCSFME LHYSCNGFEY GGYMKDTGFP LTERDRLGLR GLLPPRVISF
EQQYDRFMNS YRSLEKNTHG QPDKVVALAK WRILNRLHDR NETLYYRVDM IMIVLTNGSR
ILGLGDLGVQ GIGIPIGKLD IYVAAAGISL QGILPVMLDV GTSNQKLLED RLYLGLRQPR
LEGEEYLSIV DEFMEAVHAR WPKAIVQGTA GVALAGILGS VRAQGRPLSD FVNQRIVVVG
AGSAGLGVLK MAIQAVSKMA GCSETAAKSQ FFLIDKDACF HIFTSFGLVT TDRNNLDPAA
APFAKNPRDL EGLTEGASII EVVKKVRPHV LLGLSGVGGI FNEEVLKAMK ESVSTKPAIF
AMSSPTMNAE CTAIDAFKHA GGDIVFGSGS PFENVDLGN
//
