ID A0A329ZES2_9HELI Unreviewed; 473 AA.
AC A0A329ZES2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Pyruvate carboxylase subunit A {ECO:0000313|EMBL:RAX53863.1};
DE EC=6.4.1.1 {ECO:0000313|EMBL:RAX53863.1};
GN ORFNames=CCY99_05635 {ECO:0000313|EMBL:RAX53863.1};
OS Helicobacter sp. 16-1353.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=2004996 {ECO:0000313|EMBL:RAX53863.1, ECO:0000313|Proteomes:UP000251728};
RN [1] {ECO:0000313|EMBL:RAX53863.1, ECO:0000313|Proteomes:UP000251728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-1353 {ECO:0000313|EMBL:RAX53863.1,
RC ECO:0000313|Proteomes:UP000251728};
RX PubMed=29225701; DOI=10.1186/s13099-017-0220-y;
RA Feng Y., Mannion A., Madden C.M., Swennes A.G., Townes C., Byrd C.,
RA Marini R.P., Fox J.G.;
RT "Cytotoxic Escherichia coli strains encoding colibactin and cytotoxic
RT necrotizing factor (CNF) colonize laboratory macaques.";
RL Gut Pathog. 9:71-71(2017).
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:RAX53863.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NHYM01000007; RAX53863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A329ZES2; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000251728; 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; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:RAX53863.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:RAX53863.1}.
FT DOMAIN 1..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 473 AA; 52572 MW; 1193E480D85727BF CRC64;
MFSKILIANR GEIAVRIIRA CNDLHIKSVA IYSRADKESM HVKMASESYE VSQDPLKSYL
DGDAIIDIAL ACDAEAIHPG YGFLSENAEF AQKVKDAGLV WIGPDASVIA KMGDKNAARE
LMKKNGIPIV PGTDALNNHS IQEIKIMANK IGYPVILKAS NGGGGRGIRV VRNDSEIEEN
LAACKREAMA FFKNDEVFME KCIENPKHIE FQILGDNYGN IIHLLERDCS IQRRHQKLVE
IAPSPTMSLD LRRRMGAVAV AAAKAANYTN AGTIEFLVDD LGNFYFMEMN TRIQVEHGIT
EEITGFDLIG RQIRSAAGEI LDLNQNEVIH QGYAIEVRIN AEDVKNDFTP NPGKITTYYP
SLGPFVRIDS SVYKDYTIPP HYDSMIAKLM VRASSYDLAV NKLIRALDEF TIRGIKTTIP
FLLNIAKDKD FRKGNFDTSY LESNMQRLMP SEIINKDDIA TAIAAAIAIR AGY
//
