ID X7EJP7_9RHOB Unreviewed; 1146 AA.
AC X7EJP7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=OCH239_08095 {ECO:0000313|EMBL:ETX16110.1};
OS Roseivivax halodurans JCM 10272.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449350 {ECO:0000313|EMBL:ETX16110.1, ECO:0000313|Proteomes:UP000022447};
RN [1] {ECO:0000313|EMBL:ETX16110.1, ECO:0000313|Proteomes:UP000022447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10272 {ECO:0000313|EMBL:ETX16110.1,
RC ECO:0000313|Proteomes:UP000022447};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax halodurans JCM 10272 Genome Sequencing.";
RL Submitted (JAN-2014) 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:ETX16110.1}.
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DR EMBL; JALZ01000002; ETX16110.1; -; Genomic_DNA.
DR RefSeq; WP_037258616.1; NZ_JALZ01000002.1.
DR AlphaFoldDB; X7EJP7; -.
DR STRING; 1449350.OCH239_08095; -.
DR PATRIC; fig|1449350.3.peg.658; -.
DR eggNOG; COG1038; Bacteria.
DR OrthoDB; 9763189at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000022447; 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:ETX16110.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000022447}.
FT DOMAIN 3..456
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 533..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 REGION 482..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 542
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 614
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 1146 AA; 126006 MW; CC44D9540D830D80 CRC64;
MADFQKILIA NRGEIAIRIM RAANEMGKKT VAVFAEEDKL GLHRFKADEA YRIGEGLGPV
QAYLSIPEII RVAKLSGADA IHPGYGLLSE NPEFVDACDK AGITFIGPRA ETMRALGDKA
SARRVAMEAG VPVVPATEVL GDDMDKIRAE AAEIGYPLML KASWGGGGRG MRPINSEDEL
ADKVKEGRRE AEAAFGNGEG YLEKMIERAR HVEVQILGDK QGNIYHLYER DCSVQRRNQK
VVERAPAPYL SAAQREELCE LGRKICAHVN YECAGTVEFL MDMDTGQFYF IEVNPRVQVE
HTVTEEVTGI DIVQAQILIA EGKSLTEATG KASQYDVSLN GHALQTRITT EDPTNNFIPD
YGRITAYRSA TGMGIRLDGG TAYAGGVITR FYDSLLVKVT AWAPTPEKAI ARMDRALREF
RIRGVSTNID FVANLLRHPT FLSNQYTTKF IDTTPELFDF KPRRDRGTKV LTYIADITVN
GHPETEGRTK PAADIKVPRA PETSGSAPDG TRQLLDREGP QAVADWLAAQ KQVLITDTTM
RDGHQSLLAT RMRSIDMVRV APAYAENLSG LFSVECWGGA TFDVAYRFLQ ECPWQRLRDI
RARMPNIMTQ MLLRASNGVG YTNYPDNVVR SFVHRAAESG VDVFRVFDSL NWTENMRVAM
DAVLESGKVC EGAICYTGDI NDPDRAKYDL KYYVSMGKEL REAGAHILGL KDMAGLLKPA
AAGPLIRALK EEVGLPVHFH THDTSGAAIA SVMAAAEAGV DAVDAAMDAL SGNTSQPTLG
SIVEALRFTE RETGLDIKRI REISNYWEQV RAQYAAFESA MQSPASEVYL HEMPGGQFTN
LRAQARSLGL EDKWPEVART YADVNQMFGD IVKVTPSSKV VGDMALMMVS QGLTRAEVED
PKRDISFPDS VIDMMKGNLG HPPGGFPEGI QKKVLKGEKP LEDRPGKHLP PVDLDDKRRE
LAEAFEDVEF DEEDLNGYLM YPKVFTDYVA RHELYGPVRT LPTKTFFYGM TPGEEVTAEI
DPGKTLEIRL VTVGESNEGE VRVFFELNGQ PRTVRVPDRK ATGGAAARPK AELGNAAHVG
APMPGVVSQV AAEAGKPVKE GDLLLVIEAM KMETGLYAER DATVKAVHVH AGGQIDAKDL
LIEYEE
//
