ID   Q2PQV1_PSEPI            Unreviewed;       232 AA.
AC   Q2PQV1;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Plastid acetyl-CoA carboxylase {ECO:0000313|EMBL:ABC18242.1};
DE   Flags: Fragment;
OS   Pseudoroegneria spicata (Bluebunch wheatgrass) (Agropyron spicatum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Pseudoroegneria.
OX   NCBI_TaxID=4604 {ECO:0000313|EMBL:ABC18242.1};
RN   [1] {ECO:0000313|EMBL:ABC18242.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Fan X., Zhou Y.H., Sha L.N., Liu D.C., Zheng Y.L.;
RT   "Phylogenetic relationships of the monogenomic species of the tribe,
RT   Triticeae (Poaceae), inferred from gene encoding plastid acetyl-CoA
RT   carboxylase.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DQ306262; ABC18242.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2PQV1; -.
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:ABC18242.1"
FT   NON_TER         232
FT                   /evidence="ECO:0000313|EMBL:ABC18242.1"
SQ   SEQUENCE   232 AA;  25836 MW;  3F99C1D284801455 CRC64;
     QSRHLEVQLL CDQYGNVAAL HSRDCSVQRR HQKIIEEGPV TVAPRETVKE LEQAARRLAK
     AVGYVGAATV EYLYSMETGE YYFLELNPRL QVEHPVTEWI AEVNLPAAQV AVGMGIPLWQ
     VPEIRRFYGM DNGGGYDIWR KTAALATPFN FDEVDSQWPN GHCVAVRITS EDPDDGFKPT
     GGKVKEISFK SKPNVWAYFS VKSGGGIHEF ADSQFGHVFA YGVSRAAAIT NM
//