ID D4XBC6_9BURK Unreviewed; 623 AA.
AC D4XBC6;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Phosphoenolpyruvate carboxykinase [GTP] {ECO:0000256|HAMAP-Rule:MF_00452};
DE Short=PEP carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
DE Short=PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
DE EC=4.1.1.32 {ECO:0000256|HAMAP-Rule:MF_00452};
DE AltName: Full=GTP-dependent phosphoenolpyruvate carboxykinase {ECO:0000256|HAMAP-Rule:MF_00452};
DE Short=GTP-PEPCK {ECO:0000256|HAMAP-Rule:MF_00452};
GN Name=pckA {ECO:0000313|EMBL:EFF75712.1};
GN Synonyms=pckG {ECO:0000256|HAMAP-Rule:MF_00452};
GN ORFNames=HMPREF0004_2773 {ECO:0000313|EMBL:EFF75712.1};
OS Achromobacter piechaudii ATCC 43553.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=742159 {ECO:0000313|EMBL:EFF75712.1, ECO:0000313|Proteomes:UP000004510};
RN [1] {ECO:0000313|Proteomes:UP000004510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43553 {ECO:0000313|Proteomes:UP000004510};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
CC phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC pathway that produces glucose from lactate and other precursors derived
CC from the citric acid cycle. {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00452};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00452};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00452};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452}.
CC -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC family. {ECO:0000256|ARBA:ARBA00005796, ECO:0000256|HAMAP-
CC Rule:MF_00452}.
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:EFF75712.1}.
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DR EMBL; ADMS01000062; EFF75712.1; -; Genomic_DNA.
DR AlphaFoldDB; D4XBC6; -.
DR PATRIC; fig|742159.3.peg.3708; -.
DR eggNOG; COG1274; Bacteria.
DR HOGENOM; CLU_028872_1_1_4; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000004510; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00819; PEPCK_GTP; 1.
DR Gene3D; 3.90.228.20; -; 1.
DR Gene3D; 3.40.449.10; Phosphoenolpyruvate Carboxykinase, domain 1; 1.
DR Gene3D; 2.170.8.10; Phosphoenolpyruvate Carboxykinase, domain 2; 1.
DR HAMAP; MF_00452; PEPCK_GTP; 1.
DR InterPro; IPR013035; PEP_carboxykinase_C.
DR InterPro; IPR008209; PEP_carboxykinase_GTP.
DR InterPro; IPR035077; PEP_carboxykinase_GTP_C.
DR InterPro; IPR035078; PEP_carboxykinase_GTP_N.
DR InterPro; IPR008210; PEP_carboxykinase_N.
DR PANTHER; PTHR11561; PHOSPHOENOLPYRUVATE CARBOXYKINASE; 1.
DR PANTHER; PTHR11561:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP)-RELATED; 1.
DR Pfam; PF00821; PEPCK_GTP; 1.
DR Pfam; PF17297; PEPCK_N; 1.
DR PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR SUPFAM; SSF53795; PEP carboxykinase-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00452};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00452};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_00452};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00452}; Kinase {ECO:0000313|EMBL:EFF75712.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00452};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00452};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00452};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00452}; Pyruvate {ECO:0000313|EMBL:EFF75712.1};
KW Transferase {ECO:0000313|EMBL:EFF75712.1}.
FT DOMAIN 30..250
FT /note="Phosphoenolpyruvate carboxykinase GTP-utilising N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17297"
FT DOMAIN 254..617
FT /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop"
FT /evidence="ECO:0000259|Pfam:PF00821"
FT ACT_SITE 282
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 229..231
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 238
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 281..286
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 307
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 401..403
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 403
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 531..534
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
SQ SEQUENCE 623 AA; 68285 MW; D0DE3EB2CD5C2081 CRC64;
MEIAPMNKPL DGGLAALNVP AYVKHRGLID WVASFVALAK PDRVVWCDGS QEEYDRLCEQ
MVQAGTMRRL NPAKRPNSFL ACSDPSDVAR VEDRTFICSD RAEDAGPTNN WADPAEMRDT
LNGLFDGAMR GRTLYVVPFS MGPLGSDIAH IGVELSDSPY VVVNMRIMTR MGKAVYDVLG
TDGDFVPCVH SVGKPLAAGE ADVPWPCNPT KYIVHFPKSR EIWSYGSGYG GNALLGKKCF
ALRIASTMGR DQGWLAEHML ILGVTSPKGR KYHVAAAFPS ACGKTNFAML IPPQGMDGWK
VTTIGDDIAW IKPGPDGRLH AINPEAGYFG VAPGTSEQTN FNAMATLKAN VIFTNVALTD
DGDVWWEGMT DTPPAHLIDW QGQDWTPAIA RETGRKAAHP NARFTAPAAQ CPSIDPEWEN
PKGVVIDAFI FGGRRSTTVP LVTEARNWVE GVYMAATMGS ETTAAAVGQQ GVVRRDPFAM
LPFCGYNMSD YFNHWLKLGK QLEAAGATLP RIYCVNWFRK GPDGKFVWPG FGENMRVLRW
MLGRIDGESK GVDQVFGVSP SYQDIDWTGL EFTPDKFEQV MSVDAAAWRD ELALHHELFG
QLSQGLPEDL PATKTKIEGR LVA
//
