ID A0A0S7XGL9_9BACT Unreviewed; 499 AA.
AC A0A0S7XGL9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Pyruvate carboxylase subunit A {ECO:0000313|EMBL:KPJ61601.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:KPJ61601.1};
GN ORFNames=AMJ46_00420 {ECO:0000313|EMBL:KPJ61601.1};
OS Latescibacteria bacterium DG_63.
OC Bacteria; Candidatus Latescibacteria.
OX NCBI_TaxID=1703781 {ECO:0000313|EMBL:KPJ61601.1, ECO:0000313|Proteomes:UP000051457};
RN [1] {ECO:0000313|EMBL:KPJ61601.1, ECO:0000313|Proteomes:UP000051457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG_63 {ECO:0000313|EMBL:KPJ61601.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPJ61601.1}.
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DR EMBL; LJNC01000002; KPJ61601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S7XGL9; -.
DR PATRIC; fig|1703781.3.peg.92; -.
DR Proteomes; UP000051457; Unassembled WGS sequence.
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:UniProtKB-EC.
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; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KPJ61601.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:KPJ61601.1}.
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 499 AA; 55097 MW; D20C2437E5C23E65 CRC64;
MKKILVANRG EIALRVMKAC HEMDVPTVAV YSTSDKGSLH VQFADEAVCI GPPPPLESYL
NIERLLSTAK ERGADAIHPG YGFLAENSDF ARRCSEEGIT FIGPGHEAMR LLGNKVESRK
TMVEAGIPVI PGMMRAGKDV GSLRKEATEM GLPVLVKAAG GGGGKGMRIV REEKELEDSL
SACMREAKSA FGDDTIYLER YIERPRHIEF QILADCHGNV VHLFERECSI QRRYQKIVEE
TPSVALDPGL REKMGRVAVK VAETAGYTNA GTVEFLLDEK REFYFLEVNA RVQVEHPITE
AVVGVDLVKQ QIRIASGEKL LLKQEELRQR GHAIECRIYA EDPENNFLPC AGKILFVKEP
EGPGIRCDSG IWSGCEVSVH YDPILSKLVV WDETREQACK RMTAALKRYA ILGIKTTTSF
LAAVMEHPAF HEGKTHTGFI ADHFWDWRSP EGDGSGLRIA LLAAAALEKK APARRAPGAV
AETFSPWKSG TKWRIGGNS
//
