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Database: UniProt
Entry: A0A317ZQC7_9BACT
LinkDB: A0A317ZQC7_9BACT
Original site: A0A317ZQC7_9BACT 
ID   A0A317ZQC7_9BACT        Unreviewed;      1145 AA.
AC   A0A317ZQC7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=DDZ13_01745 {ECO:0000313|EMBL:PXA05621.1};
OS   Coraliomargarita sinensis.
OC   Bacteria; Verrucomicrobiota; Opitutae; Puniceicoccales;
OC   Coraliomargaritaceae; Coraliomargarita.
OX   NCBI_TaxID=2174842 {ECO:0000313|EMBL:PXA05621.1, ECO:0000313|Proteomes:UP000247099};
RN   [1] {ECO:0000313|EMBL:PXA05621.1, ECO:0000313|Proteomes:UP000247099}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WN38 {ECO:0000313|EMBL:PXA05621.1,
RC   ECO:0000313|Proteomes:UP000247099};
RA   Zhou L.Y.;
RT   "Coraliomargarita sinensis sp. nov., isolated from a marine solar
RT   saltern.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC       carboxylation of the covalently attached biotin in the first step and
CC       the transfer of the carboxyl group to pyruvate in the second.
CC       {ECO:0000256|PIRNR:PIRNR001594}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC         + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.4.1.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953,
CC         ECO:0000256|PIRNR:PIRNR001594};
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:PXA05621.1}.
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DR   EMBL; QHJQ01000001; PXA05621.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317ZQC7; -.
DR   InParanoid; A0A317ZQC7; -.
DR   OrthoDB; 9807469at2; -.
DR   Proteomes; UP000247099; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
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; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR01235; pyruv_carbox; 1.
DR   PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594};
KW   Biotin {ECO:0000256|PIRNR:PIRNR001594};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:PXA05621.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247099}.
FT   DOMAIN          1..454
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          120..318
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          532..801
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1070..1145
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   ACT_SITE        293
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         541
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         613
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         711
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         740
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         742
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         875
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         711
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1111
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1145 AA;  127194 MW;  EA9152751E650AC7 CRC64;
     MTKLLAANRS EIAVRIFRSA TELGCRTVSI YANEDRFGVH RFKADESYLV GEGKGPVAAY
     LDIESIIDLA KDKAVDLIHP GYGFLSENAG FAKACEENGI TFVGPSAELL SRMGDKIEAR
     KIADKAKVPT LPGTKDPISD PDKALKTAMK IGFPLIIKAA FGGGGRGMRV VKDPKDLKSS
     LEEAQGEAER AFGNSAVFLE RYIEKAKHIE VQILGDQQGN VVHLHERDCS VQRRHQKVVE
     IAPSIGLPDA VRAELCQAAV QIAKSIGYYS AGTVEFLYDL ETDEWFFIEM NPRIQVEHTV
     TEVITGIDIV RSQILVAQGH SLHGEEIGIP QQENIPRNGV AIQARITTED PESNFAPDYG
     KIVNYRSAAG FGIRLDGAMG DTGAVITPYY DSLLVKLTAS ARTFELAIQR MDRALREMRI
     RGVKTNIPFI ENVINHPIFV SGKATTTLID TSKELFNFKR RKDRATKLLK LLGDTIVNGN
     DQVKDRPVPT MDLPVIVPKY DHRHGLPRGT KDYLDRHGPE KFAEWTRKQK KLLVTDTTMR
     DAHQSLLAAR MRSYDQLKVA DAIAHRAGDL YSLECWGGAT FDTSMRFLRE NPFKRLRRLR
     ERIPNVCFQM LLRGANGVGY SNYPDNVIRE FIKHSAESGM DIFRVFDSLN YLPNLKVAME
     SIRKHTNSVC EGTICYTGDI LDPKRDKYSL EYYVKMAKEL ESMGAHILAL KDMSGLCTPH
     AAYKLIKTLR SEIGIPVHFH THDSSGIAGA SIIKAAEAGV DVVDLAVSSL SGLTSQPNLN
     STVNALQGDK RDTKLDLKFL NELSIYWEAI RQYYEPFDTA PKFGSAEVYT HEMPGGQYTN
     LREQARALGL GTRWPEVVRY YHEVNMVLGD IVKVTPSSKV VGDLAMFLLT KGIEPKDLVN
     LEPGGDFPES VVDMLSGGLG QPKGGWPKKV QKVILGDKKP YKGRPGARAE KVDLDATRKE
     LAKKYKCEIS DDDLYAYLMY PQVFADLKKY VDEYGHARVL PTPAFFYGLK PGEEISVEIE
     EGKVLIVKLI YVSEPNGDGE RTLTFELNGR ARECVILDRS IKADTKKRTK ADSGDKMQVG
     APIPAMVSSV SVSVGQKVKK KEKLCVLEAM KMQTTVYALA DGTVDTIEVQ AGDQVDSKDL
     LVRLR
//
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