ID B7U8F2_9POAL Unreviewed; 232 AA.
AC B7U8F2;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Plastid acetyl-CoA carboxylase {ECO:0000313|EMBL:ACK57302.1};
DE Flags: Fragment;
GN Name=Acc1 {ECO:0000313|EMBL:ACK57302.1};
OS Leymus karelinii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Hordeinae; Leymus.
OX NCBI_TaxID=363597 {ECO:0000313|EMBL:ACK57302.1};
RN [1] {ECO:0000313|EMBL:ACK57302.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1 {ECO:0000313|EMBL:ACK57302.1};
RX PubMed=19814813; DOI=10.1186/1471-2148-9-247;
RA Fan X., Sha L.N., Yang R.W., Zhang H.Q., Kang H.Y., Ding C.B., Zhang L.,
RA Zheng Y.L., Zhou Y.H.;
RT "Phylogeny and evolutionary history of Leymus (Triticeae; Poaceae) based on
RT a single-copy nuclear gene encoding plastid acetyl-CoA carboxylase.";
RL BMC Evol. Biol. 9:247-247(2009).
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DR EMBL; FJ449607; ACK57302.1; -; Genomic_DNA.
DR AlphaFoldDB; B7U8F2; -.
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:ACK57302.1"
FT NON_TER 232
FT /evidence="ECO:0000313|EMBL:ACK57302.1"
SQ SEQUENCE 232 AA; 25806 MW; 2F6764699A25A7D5 CRC64;
QSRHLEVQLL CDQYGNVAAL HSRDCSVQRR HQKIIEEGPV TVAPRETVKE LEQAARRLAK
AVGYVGAATV EYLYSMETGE YYFLELNPRL QVEHPVTEWI AEVNLPAAQV AVGMGIPLWQ
VPEIRRFYGM DNGGGCDIWR KTAALATPFN FDEVDSQWPK GHCVAVRITS EDPDDGFKPT
GGKVKEISFK SKPNVWAYFS VKSGGGIHEF ADSQFGHVFA YGVSRSAAIT NM
//
