ID A0A2T5MGK4_9GAMM Unreviewed; 1150 AA.
AC A0A2T5MGK4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=CJD38_10305 {ECO:0000313|EMBL:PTU31693.1};
OS Stenotrophobium rhamnosiphilum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Stenotrophobium.
OX NCBI_TaxID=2029166 {ECO:0000313|EMBL:PTU31693.1, ECO:0000313|Proteomes:UP000244248};
RN [1] {ECO:0000313|EMBL:PTU31693.1, ECO:0000313|Proteomes:UP000244248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GT1R17 {ECO:0000313|EMBL:PTU31693.1,
RC ECO:0000313|Proteomes:UP000244248};
RA Liu Q., Xin Y.-H.;
RT "Novel species isolated from glacier.";
RL Submitted (APR-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:PTU31693.1}.
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DR EMBL; QANS01000003; PTU31693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T5MGK4; -.
DR OrthoDB; 9760256at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000244248; 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: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}; Pyruvate {ECO:0000313|EMBL:PTU31693.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244248}.
FT DOMAIN 5..457
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 536..804
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1073..1148
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 298
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 545
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 617
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 714
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
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 745
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 878
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 714
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1114
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1150 AA; 125903 MW; 4ADA4AA0715586F6 CRC64;
MSSKKIEKIL VANRGEISIR IMRAAAEMDI RTVSIYAYED RFALHRFKAD ESYKVGNGQK
PIAAYLDIAD IIRVAKAANV DAIHPGYGFL SENPNLADAC AEAGIRFIGP NSTVLRTLGD
KVAARTAAIA AKVPVLPASG ALPQDVEACK PIVAKVGYPV MMKASWGGGG RGMRVIENEA
ELGPQMASAR SEAKSAFGND EVYVEKLVRR ARHVEVQVLA DTHGNLMHLF ERDCSVQRRN
QKVVERAPAP YLDEARRQML CDSALRLCKQ VGYSHAGTVE FLMDADTGEF YFIEVNPRIQ
VEHTVTEEVT GVDIVKAQIR VTEGLKLGEG GLPTQDQVRL DGHALQCRVT TEDPENGFTP
DHGRLTAYRS PAGFGIRLDG GTAYGGAIVT PFYDSMLVKL TAWAPTADEA VNRMDRALRE
FRIRGVSTNL QFLENVIGHE EFRAGTCITK FIDNTPELFR FTPRRDRATK LLRFIGEVIV
NGNPEMKGRK IPDTAFVAPP LPPISLALPP PRGMRDELIE RGPAGFAQWM KAEKKVLLTD
TTMRDAHQSL FATRMRSADM AAIAPYYARL APQLFSVECW GGATFDVAMR FLKEDPWERL
STLRAAIPNI PFQMLLRSAN AVGYTNYADN VVRYFVQQAA KNGIDIFRVF DSLNSVDNMR
VAMDAVIESG AVCEAAICYT GDLFDGARPK YNLQYYVKMA KALEKSGAHI LGIKDMAGIC
RPRAARELVR VLKEETGLPI HFHTHDTSGI SAASVLAAIE AGCDAVDGAL DSMSGLTSQP
NLGAIAASLS GSDRDPRIDF DALQQLSNYW EGVRRYYAPF EADIRSGTAD VYRHEMPGGQ
YTNLREQARS LGLEQRWPEV SKAYADVNKL FGDIVKVTPT SKVVGDMALF MVGNNLTPEQ
VLSPETSVDF PESVVSLMRG ELGFPPEGFP AQLQQKILKG KPPLVGRPGA SLPPVDLEKT
RNDAQKALGE KLSDTDLASH LMYPKVFRDF VEHRKTYGEL SALPTPAFFY GLREREEISV
DIERGKTLVI RLQGSSDVEE EGIAKLFYEL NGQPRMVRIP LAGAAGAKAA RAKADEGNPA
HIGAPMPGMV VRIAAQKGSR VAKGEPLVAI EAMKMETIVA APREGIIKDI LVVAGVTIAA
KDLLVIIEPV
//
