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
//