ID C1DH59_AZOVD Unreviewed; 471 AA.
AC C1DH59;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Pyruvate carboxylase subunit A {ECO:0000313|EMBL:ACO76466.1};
GN Name=pycA {ECO:0000313|EMBL:ACO76466.1};
GN OrderedLocusNames=Avin_02050 {ECO:0000313|EMBL:ACO76466.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO76466.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO76466.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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DR EMBL; CP001157; ACO76466.1; -; Genomic_DNA.
DR RefSeq; WP_012698894.1; NC_012560.1.
DR AlphaFoldDB; C1DH59; -.
DR STRING; 322710.Avin_02050; -.
DR EnsemblBacteria; ACO76466; ACO76466; Avin_02050.
DR KEGG; avn:Avin_02050; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF1; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 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; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:ACO76466.1}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 471 AA; 51766 MW; 816388E627E318B9 CRC64;
MIKKILIANR GEIAVRIVRA CAEMGIRSVA IYSEADRHAL HVKRADEAYF IGEDPLAGYL
NPRKLVNLAM ETGCDALHPG YGFLSENAEL AEICAERGIK FIGPSASVIR RMGDKTEARR
SMIAAGVPCT PGTEGNVADL AEALLEAERI GYPVMLKATS GGGGRGIRRC NSAAELENAY
PRVISEATKA FGSAEVFLEK CIVNPKHIEA QVLADSFGNT VHLFERDCSI QRRNQKLIEI
APSPQLTPEQ RAYIGDLAVR AARAVGYENA GTVEFLLADG EVYFMEMNTR VQVEHTITEE
ITGIDIVREQ IRIASGLPLS VEQKDIQHRG YALQFRINAE DPKNNFLPSF GKITRYYAPG
GPGVRTDTAI YTGYTIPPYY DSMCLKLIVW ALTWEEALAR GLRALDDMRV QGVKTTAPYY
QQILGNPDFR SGQFNTSFVD EHPELLDYSI KRRPGELAIA IAAAIAAHAG L
//
