ID C9LQ62_9FIRM Unreviewed; 1142 AA.
AC C9LQ62;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 60.
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 Name=pyc {ECO:0000313|EMBL:EEW97698.1};
GN ORFNames=GCWU000321_01694 {ECO:0000313|EMBL:EEW97698.1};
OS Dialister invisus DSM 15470.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Dialister.
OX NCBI_TaxID=592028 {ECO:0000313|EMBL:EEW97698.1, ECO:0000313|Proteomes:UP000004736};
RN [1] {ECO:0000313|EMBL:EEW97698.1, ECO:0000313|Proteomes:UP000004736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15470 {ECO:0000313|EMBL:EEW97698.1,
RC ECO:0000313|Proteomes:UP000004736};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEW97698.1}.
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DR EMBL; ACIM02000001; EEW97698.1; -; Genomic_DNA.
DR RefSeq; WP_007070629.1; NZ_GG698602.1.
DR AlphaFoldDB; C9LQ62; -.
DR STRING; 592028.GCWU000321_01694; -.
DR GeneID; 78278219; -.
DR eggNOG; COG1038; Bacteria.
DR HOGENOM; CLU_000395_0_1_9; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000004736; 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; 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:EEW97698.1}.
FT DOMAIN 3..457
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 534..802
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1067..1142
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 543
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 615
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 712
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 741
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 743
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 876
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 712
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1108
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1142 AA; 127931 MW; F874C171FC068D1B CRC64;
MRKIRKVLVA NRGEIAIRVF RACNELGIRT VAVYSKEDVL SLHRNRADEA YLVGEGDKPI
DAYLDIEDII RICKEHHVDA VHPGYGFLAE NAELAKRCEE EGIIFIGPRV EHLIMFGDKV
NARIQAEKAQ IPMIPGTNGA VESFDEVKAF AEEYGFPVMI KAVNGGGGRG MRNVDRMEDL
EEAYHRAKSE AKMAFGSDEV YVEKCIMNPK HIEVQILGDE AGHVIHLFER DCSIQRRHQK
VIEMAPAWSL PQKLREDICS AAVKLMKNVN YLNAGTVEFL VDQDEEHFYF IEVNPRVQVE
HTVTEMITDV DIVKTQILIA EGYSVDSPEV AIGLQPTIWF KGVAIQCRIT TEDPQNGFMP
DTGKIIAYRS GGGPGIRLDA GTAYTGAVIT PYYDSLLVKV TAHALHAKDT VHRMLRCLDE
FRISGVKTNI YFLQNMLRTK DFQEGLCDVN YIDRHPQLLD EPEAISDRGT KLLRYIGDIT
VNGYAGAGAK EKPDFAPAAP LSAEGETVPR GTRQMLEKWG PEKFSKWVMD QKELMIMDTT
YRDAHQSLLA TRVRTHDIMN AIRYTACHVP QLFSFENWGG ATFDVAYRFL DESPWERLRR
MREAAPNILF QMLTRGANTV GYTNYPENVV RHFIDEAADN GIDVFRIFDC LNQLSHMTIS
IDEVRKKGKL AEACFCYTGD IMDPKRQKYS LKYYTDLAKE MQNAGANLIA VKDMAGLLKP
EAAYALVAAL KDAVDLPIHL HSHEGGGLTL YSYAKAAEAG VDIVDVATGA LSNGTSQPSM
TALYYALQNN PRQPKLDIEA LETIDRYWQG IRPYYAGVDS RMASPNTTLF QHEMPGGQFS
NLRQQATAVG LGDRWPEVCR MYARVNMMFG DIIKVTPSSK VVGDMTLFMV QNHLMEEDIY
EKGAALDFPQ SVVDFFDGKL GVPYGGFPEK LQKIILRGEE PHLESHPQDV DFAAVKAEMK
GRHMSTREED ISSYCIYPKV FSDYMDRYHQ YGDLSVLDTP TFFFGMKPGE EIRVNIEEGK
MLLIRLDGIT KPDGEGNRRI QFELNGMPRE IKIHDRHVAE SAVTARKADK DIPGEVGATL
SGSVVKVLAE KGGHVKKGEP VIVTEAMKME TTITSPVDGI VSEIHVKAGS RIESGDLLMV
IE
//
