ID L7Z888_BACTU Unreviewed; 267 AA.
AC L7Z888;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Pyruvate carboxylase {ECO:0000313|EMBL:AGE09789.1};
DE Flags: Fragment;
GN Name=pycA {ECO:0000313|EMBL:AGE09789.1};
OS Bacillus thuringiensis serovar oswaldocruzi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=180872 {ECO:0000313|EMBL:AGE09789.1};
RN [1] {ECO:0000313|EMBL:AGE09789.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IEBC-T38 001 {ECO:0000313|EMBL:AGE09789.1};
RX PubMed=23475137; DOI=10.1007/s00284-013-0339-0;
RA Soufiane B., Cote J.C.;
RT "Discrimination Between Mesophilic and Psychrotolerant Strains in the
RT Bacillus cereus Group Based on the PstI Digestion of the pycA Gene.";
RL Curr. Microbiol. 67:148-155(2013).
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DR EMBL; KC196950; AGE09789.1; -; Genomic_DNA.
DR AlphaFoldDB; L7Z888; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 6.10.140.310; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005930; Pyruv_COase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 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; 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|PROSITE-ProRule:PRU00409};
KW Pyruvate {ECO:0000313|EMBL:AGE09789.1}.
FT DOMAIN 1..267
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 15..209
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGE09789.1"
FT NON_TER 267
FT /evidence="ECO:0000313|EMBL:AGE09789.1"
SQ SEQUENCE 267 AA; 29812 MW; F76F6E13384155BA CRC64;
KHLDMFGDKV KARTQAQLAQ IPVIPGSDGP VDSLEEVKEF AEKYDYPIII KASLGGGGRG
MRIVRTSEEL RESYNRAKSE AKAAFGNDEV YVEKFVEKPK HIEVQILADE EGNVVHLYER
DCSVQRRHQK VVEIAPSVSL SDDLRQRICE AAVKLTKNVN YLNAGTVEFL VKDDNFYFIE
VNPRVQVEHT ITEMITGVDI VQSQILIADG HALHSKMVGV PKQEEVVVHG FAIQSRVTTE
DPLNNFMPDT GKIMAYRSGG GFGVRLD
//
