ID E3ULG8_9POAL Unreviewed; 268 AA.
AC E3ULG8;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Plastid acetyl-CoA carboxylase {ECO:0000313|EMBL:ADP00634.1};
DE Flags: Fragment;
GN Name=Acc1 {ECO:0000313|EMBL:ADP00634.1};
OS Festuca circummediterranea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Poodae; Poeae; Poeae Chloroplast Group 2 (Poeae type);
OC Loliodinae; Loliinae; Festuca.
OX NCBI_TaxID=906890 {ECO:0000313|EMBL:ADP00634.1};
RN [1] {ECO:0000313|EMBL:ADP00634.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20937141; DOI=10.1186/1471-2148-10-303;
RA Hand M.L., Cogan N.O., Stewart A.V., Forster J.W.;
RT "Evolutionary history of tall fescue morphotypes inferred from molecular
RT phylogenetics of the Lolium-Festuca species complex.";
RL BMC Evol. Biol. 10:303-303(2010).
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DR EMBL; HM453089; ADP00634.1; -; Genomic_DNA.
DR AlphaFoldDB; E3ULG8; -.
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 SMART; SM00878; Biotin_carb_C; 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 1..268
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 57..129
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADP00634.1"
FT NON_TER 268
FT /evidence="ECO:0000313|EMBL:ADP00634.1"
SQ SEQUENCE 268 AA; 29818 MW; 2AC7A692AA443496 CRC64;
VPGSPIFIMR LASQSRHLEV QLLCDQYGNV AALHSRDCSV QRRHQKIIEE GPVTVAPRET
VKELEQAARR LAKAVGYVGA ATVEYLYSME TGEYYFLELN PRLQVEHPVT EWIAEVNLPA
AQVAVGMGIP LWQVPEIRRF YGMDNGGGYD IWRKTAALAT PFNFDEVDSQ WPKGHCVAVR
ITSENPDDGF KPTGGKVKEI SFKSKPNVWG YFSVKSGGGI HEFADSQFGH VFAYGVTRSA
AITSMSLALK EIQIRGEIHT NVDYTVDL
//
