ID A0A3A3G6Q3_9BURK Unreviewed; 1157 AA.
AC A0A3A3G6Q3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=D3878_13225 {ECO:0000313|EMBL:RJG02419.1};
OS Noviherbaspirillum sedimenti.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=2320865 {ECO:0000313|EMBL:RJG02419.1, ECO:0000313|Proteomes:UP000266327};
RN [1] {ECO:0000313|Proteomes:UP000266327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1S02-23 {ECO:0000313|Proteomes:UP000266327};
RA Zhu H.;
RL Submitted (SEP-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 -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
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:RJG02419.1}.
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DR EMBL; QYUQ01000002; RJG02419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A3G6Q3; -.
DR OrthoDB; 9803706at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000266327; 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:UniProtKB-UniPathway.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 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|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
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};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Pyruvate {ECO:0000313|EMBL:RJG02419.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000266327}.
FT DOMAIN 10..467
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 132..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 546..814
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1082..1157
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 303
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 555
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 627
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 724
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 753
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 755
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 888
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 724
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1123
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1157 AA; 126932 MW; E2990359AE071BCC CRC64;
MIDVKVAVNP IRKILIANRS EIAIRVMRAA AELGIRTVAI YAAEDRFSLH RFKADESYLI
GEGKKPIAAY LDIDGIIRVA KEAGVDAIHP GYGFLSENPD FADACAAAGI RFVGPNSTVM
RTLGNKVAAR NAAVAADVPV MAATPALPHD LEQVIQMAAE IGYPLMLKAS WGGGGRGMRV
IESAAELPGQ LAVARREAAA AFGNDEMYLE KLVRRARHVE VQLLGDTHGK LVHLFERDCS
VQRRNQKVVE SAPAPYLDDA GRRELCEAAL RLGRAVGYTH AGTVEFLMDA DTGMFYFIEV
NPRIQVEHTV TEQVTGVDIV KAQIRITEGA HIGGDGELAC GVPLQQDIRL NGHALQCRVT
TEDPENNFTP DYGRITAYRS ASGFGIRLDG GTAYSGAVIT PYYDSLLVKV TAWAGSAEEA
IARMDRALRE FRIRGVSTNL AFLENVINHQ QFRAGQCITR FIDTTPDLFQ FSRRRDRATR
LLRFIGDVNV NGNPEMKGRT IPAQMPAPAL LPRLSADGPV VPGTRDKLKE LGAEGFSRWM
KDERRVLLTD TTMRDAHQSL FATRMRTHDM LAIAPYYARL LPNLFSLECW GGATFDVAMR
FLKEDPWERL AGLRERVPNI LFQMLLRGSN AVGYTNYADN VVRHFVGQAA AGGIDLFRVF
DSLNWVENMR VAIDAVRESG ALCEGTICYS GDMLAPTRSK YNLQYYVSMA RELERAGANI
IGIKDMAGIC KPDAARVLVR ELKETIGLPI HFHTHDTSGI SAASVLAAVD AGCDAVDGAM
DAMSGLTSQP NLGAIAAALD ASARNPEMDR QAMFEISQYW EGVRRYYAPF EADIRAGTSD
VYRHEMPGGQ YTNLREQARA MGLEHRWTDV SQTYADVNQL FGDIVKVTPT SKVVGDMALF
MVANDLTPDE VRNPDKEVAF PESVVSLFKG DLGFPPDGFP KDLEHKVLKG ELPLSGRPGA
SLPEVDLAAV RAEVEAKVAC EISEQELSSY LMYPKVFCEY AAHRHEYGNV STLPTPVFFY
GLQANQEISV DIDRGKTLIV SLHGSVEMAE EGQCKLFFEL NGQPRIVRVD RAGAVATVQH
SRAEDGNPAH VGATMPGMIV TLSVQEGQRV ARGDPLLSLE AMKMETVIRA ERDGMVRKVH
IRPGAVVSAK DLLVEFE
//