ID A1X691_9POAL Unreviewed; 229 AA.
AC A1X691;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:ABB96653.1};
DE Flags: Fragment;
GN Name=acc1 {ECO:0000313|EMBL:ABB96653.1};
OS Aegilops sharonensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=58530 {ECO:0000313|EMBL:ABB96653.1};
RN [1] {ECO:0000313|EMBL:ABB96653.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A13Sha {ECO:0000313|EMBL:ABB96653.1}, and A14Sha
RC {ECO:0000313|EMBL:ABB96654.1};
RX PubMed=17053048; DOI=10.1093/molbev/msl151;
RA Kilian B., Ozkan H., Deusch O., Effgen S., Brandolini A., Kohl J.,
RA Martin W., Salamini F.;
RT "Independent wheat B and G genome origins in outcrossing Aegilops
RT progenitor haplotypes.";
RL Mol. Biol. Evol. 24:217-227(2007).
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DR EMBL; DQ290370; ABB96653.1; -; Genomic_DNA.
DR EMBL; DQ290371; ABB96654.1; -; Genomic_DNA.
DR AlphaFoldDB; A1X691; -.
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 4..229
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 43..115
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABB96653.1"
FT NON_TER 229
FT /evidence="ECO:0000313|EMBL:ABB96653.1"
SQ SEQUENCE 229 AA; 25477 MW; 26759CE5C7058D92 CRC64;
SRHLEVQLLC DQYGNVAALH SRDCSVQRRH QKIIEEGPVT VAPRETVKEL EQAARRLAKA
VGYVGAATVE YLYSMETGEY YFLELNPRLQ VEHPVTEWIA EVNLPAAQVA VGMGIPLWQV
PEIRRFYGMD NGGGYDIWRK TAALATPFNF DEVDSQWPKG HCVAVRITSE DPDDGFKPTG
GKVKEISFKS KPNVWAYFSV KSGGGIHEFA DSQFGHVFAY GVSRAAAIT
//
