ID A0A1F1IGG0_9MICC Unreviewed; 632 AA.
AC A0A1F1IGG0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=pckG {ECO:0000256|HAMAP-Rule:MF_00452};
GN ORFNames=HMPREF2863_06865 {ECO:0000313|EMBL:OFR90428.1};
OS Micrococcus sp. HMSC067E09.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=1739367 {ECO:0000313|EMBL:OFR90428.1, ECO:0000313|Proteomes:UP000177882};
RN [1] {ECO:0000313|EMBL:OFR90428.1, ECO:0000313|Proteomes:UP000177882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC067E09 {ECO:0000313|EMBL:OFR90428.1,
RC ECO:0000313|Proteomes:UP000177882};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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|ARBA:ARBA00001936};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-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:OFR90428.1}.
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DR EMBL; LTYF01000012; OFR90428.1; -; Genomic_DNA.
DR RefSeq; WP_070639014.1; NZ_KV809441.1.
DR AlphaFoldDB; A0A1F1IGG0; -.
DR STRING; 1739367.HMPREF2863_06865; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000177882; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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:OFR90428.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00452};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00452}; Pyruvate {ECO:0000313|EMBL:OFR90428.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000177882};
KW Transferase {ECO:0000313|EMBL:OFR90428.1}.
FT DOMAIN 21..231
FT /note="Phosphoenolpyruvate carboxykinase GTP-utilising N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF17297"
FT DOMAIN 237..605
FT /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop"
FT /evidence="ECO:0000259|Pfam:PF00821"
FT REGION 67..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 211..213
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 265..270
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 392..394
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 394
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 425
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT BINDING 519..522
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
SQ SEQUENCE 632 AA; 69410 MW; F206DB0A05637A05 CRC64;
MSDPTRIQIP AEIRNESISA FVEEWARVTE PDRIELVSAV DDARLIGEAL AAGELLPAGE
GRYYARSHPK DTARSEERTV VATSESADRG SYNNWQPASE VKPLITERMR GASRGKTMYV
VPYLMAPPGT PLAAYAAGVE LTDDRKVVLQ MIRMTRVGLE HFDGLSDPDF FVRGVQVTGD
PDSLGHGTPE DARLFATIAD ERTILHYGSA YGGNALLGKI AHGLRQASYD GYSSGKFLAE
QFLLLGIRDL KTGATTHVCG GFPSASGKTN LAMALPPDAL GDRYRVDFYG DDIAWMWIDD
EGRLRAINPE NGAFGVAKDT NERTNPTAMA AIAEGSGTIF TNTAYNQLTG EVWWEGLTPQ
PPAELDGWLD WTGAPIADRG PDQQDAPWAH PNSRLTIPLE RIPNLAADAA DPAGVVIDAI
IFGGRTRDRE PLIRAIDDLA IGVYDGLTLG AEATFAAEGV DGQLRYDPMS MRPFFSYSEG
RYAQHWLTLL RQLTDLPVFA HVNWFQRDPE DGHYLWPGYR ENLRALNWLF RYRAGDAHGH
PTPVGVLPTA EELDLTGLDI PAEDLDRLLR IDTKRWTEEV QHRQEHLQGL PDVPREIWDA
HQSLSAALTA QAASADHEHP GSGPGSTHPD TH
//
