ID Q8L529_TRIDC Unreviewed; 232 AA.
AC Q8L529;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:AAM51725.1};
DE Flags: Fragment;
GN Name=Acc-1 {ECO:0000313|EMBL:AAM51725.1};
OS Triticum dicoccoides (Wild emmer) (Triticum turgidum subsp. dicoccoides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=85692 {ECO:0000313|EMBL:AAM51725.1};
RN [1] {ECO:0000313|EMBL:AAM51725.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11999851; DOI=10.1023/A:1014868320552;
RA Huang S., Sirikhachornkit A., Faris J.D., Su X., Gill B.S., Haselkorn R.,
RA Gornicki P.;
RT "Phylogenetic analysis of the acetyl-CoA carboxylase and 3-phosphoglycerate
RT kinase loci in wheat and other grasses.";
RL Plant Mol. Biol. 48:805-820(2002).
RN [2] {ECO:0000313|EMBL:AAM51725.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12060759; DOI=10.1073/pnas.072223799;
RA Huang S., Sirikhachornkit A., Su X., Faris J., Gill B., Haselkorn R.,
RA Gornicki P.;
RT "Genes encoding plastid acetyl-CoA carboxylase and 3-phosphoglycerate
RT kinase of the Triticum/Aegilops complex and the evolutionary history of
RT polyploid wheat.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8133-8138(2002).
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DR EMBL; AF343499; AAM51725.1; -; Genomic_DNA.
DR EMBL; AF343511; AAM51737.1; -; Genomic_DNA.
DR EMBL; AF343512; AAM51738.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8L529; -.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR049076; ACCA.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR45728:SF4; ACETYL-COA CARBOXYLASE 2; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 5..232
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 44..116
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAM51725.1"
FT NON_TER 232
FT /evidence="ECO:0000313|EMBL:AAM51725.1"
SQ SEQUENCE 232 AA; 25823 MW; 286700C83ECFE5BA CRC64;
QSRHLEVQLL CDQYGNVAAL HSRDCSVQRR HQKIIEEGPV TVAPRETVKE LEQAARRLAK
AVGYVGAATV EYLYSMETGE YYFLELNPRL QVEHPVTEWI AEVNLPAAQV AVGMGIPLWQ
VPEIRRFYGM DNGGGYDIWR TTAALATPFN FDEVDSQWPK GHCVAVRITS EDPDDGFKPT
GGKVKEISFK SKPNVWAYFS VKSGGGIHEF ADSQFGHVFA YGVSRAAAIT NM
//
