ID C9VZM6_9POAL Unreviewed; 232 AA.
AC C9VZM6;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Plastid acetyl-CoA carboxylase {ECO:0000313|EMBL:ACF28415.1, ECO:0000313|EMBL:AGL91077.1};
DE Flags: Fragment;
GN Name=Acc-1 {ECO:0000313|EMBL:ACF28415.1};
GN Synonyms=Acc1 {ECO:0000313|EMBL:AGL91077.1};
OS Elymus alashanicus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Elymus.
OX NCBI_TaxID=293721 {ECO:0000313|EMBL:ACF28415.1};
RN [1] {ECO:0000313|EMBL:ACF28415.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang C., Fan X., Yu H.Q., Zhang H.Q., Wang X.L., Zhou Y.H.;
RT "Phylogenetic analysis of questionable tetraploid species in Roegneria and
RT Pseudoroegneria (Poaceae: Triticeae) inferred from a gene encoding plastid
RT acety1-CoA carboxylase.";
RL Biochem. Syst. Ecol. 37:412-420(2009).
RN [2] {ECO:0000313|EMBL:AGL91077.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23816902; DOI=10.1016/j.ympev.2013.06.012;
RA Fan X., Sha L.N., Dong Z.Z., Zhang H.Q., Kang H.Y., Wang Y., Wang X.L.,
RA Zhang L., Ding C.B., Yang R.W., Zheng Y.L., Zhou Y.H.;
RT "Phylogenetic relationships and Y genome origin in Elymus L. sensu lato
RT (Triticeae; Poaceae) based on single-copy nuclear Acc1 and Pgk1 gene
RT sequences.";
RL Mol. Phylogenet. Evol. 69:919-928(2013).
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DR EMBL; EU626427; ACF28415.1; -; Genomic_DNA.
DR EMBL; KC131175; AGL91077.1; -; Genomic_DNA.
DR AlphaFoldDB; C9VZM6; -.
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:ACF28415.1"
FT NON_TER 232
FT /evidence="ECO:0000313|EMBL:ACF28415.1"
SQ SEQUENCE 232 AA; 25850 MW; 3BCC90D6D1D11455 CRC64;
QSRHLEVQLL CDQYGNVAAL HSRDCSVQRR HQKIIEEGPV TVAPRETVKE LEQAARRLAK
AVGYVGAATV EYLYSMETGE YYFLELNPRL QVEHPVTEWI AEVNLPAAQV AVGMGIPLWQ
VPEIRRFYGM DNGGGYDIWR KTAALATPFN FDEVDSQWPK GHCVAVRITS EDPDDGFKPT
GGKVKEISFK SKPNVWAYFS VKSGGGIHEF ADSQFGHVFA YGVSRAAAIT NM
//
