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Database: UniProt
Entry: A0A1Q8YHW3_9BURK
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ID   A0A1Q8YHW3_9BURK        Unreviewed;       630 AA.
AC   A0A1Q8YHW3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=BLL52_0757 {ECO:0000313|EMBL:OLP07661.1};
OS   Rhodoferax antarcticus ANT.BR.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=1111071 {ECO:0000313|EMBL:OLP07661.1, ECO:0000313|Proteomes:UP000185911};
RN   [1] {ECO:0000313|EMBL:OLP07661.1, ECO:0000313|Proteomes:UP000185911}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANT.BR {ECO:0000313|EMBL:OLP07661.1,
RC   ECO:0000313|Proteomes:UP000185911};
RA   Baker J., Riester C., Skinner B., Newell A., Swingley W., Madigan M.,
RA   Jung D., Asao M., Chen M., Loughlin P., Pan H., Lin S., Li N., Shaw J.,
RA   Prado M., Sherman C., Li X., Tang J., Blankenship R., Zhao T., Touchman J.,
RA   Sattley M.;
RT   "Genome sequence of Rhodoferax antarcticus ANT.BR, a psychrophilic purple
RT   nonsulfur bacterium from an Antarctic microbial mat.";
RL   Submitted (JAN-2017) 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:OLP07661.1}.
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DR   EMBL; MSYM01000007; OLP07661.1; -; Genomic_DNA.
DR   RefSeq; WP_075585338.1; NZ_MSYM01000007.1.
DR   AlphaFoldDB; A0A1Q8YHW3; -.
DR   STRING; 81479.RA876_17750; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000185911; 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; IPR018091; PEP_carboxykin_GTP_CS.
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, CYTOSOLIC [GTP]; 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.
DR   PROSITE; PS00505; PEPCK_GTP; 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}; Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00452};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00452}; Kinase {ECO:0000313|EMBL:OLP07661.1};
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:OLP07661.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185911};
KW   Transferase {ECO:0000313|EMBL:OLP07661.1}.
FT   DOMAIN          24..251
FT                   /note="Phosphoenolpyruvate carboxykinase GTP-utilising N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17297"
FT   DOMAIN          255..625
FT                   /note="Phosphoenolpyruvate carboxykinase C-terminal P-loop"
FT                   /evidence="ECO:0000259|Pfam:PF00821"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         230..232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         239
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         259
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         282..287
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         308
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         407..409
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         409
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         440
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
FT   BINDING         537..540
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00452"
SQ   SEQUENCE   630 AA;  69035 MW;  7A485D222CD6FD71 CRC64;
     MNTETQHDAT GQAPAYVTNQ RLIAWVAEIA ALTKPDTVYW CDGSEEEYAR LCQQLVDCGT
     FTKLNPVKRP NSFLACSDPS DVARVEDRTF ICSEKKENAG PTNNWMGPAE MRALLQTGTD
     GKKALFEGCM KGRTMYVIPF SMGPLGSPIA HIGIELSDSA YVAANMKIMT RMGKAVYDVL
     GADGAFVPCV HTVGAPLEAG QKDVTWPCNP EKYIVHYPET REIWSFGSGY GGNALLGKKC
     FALRIASNMA RDEGWLAEHM MILGATNPQG KKHYVAAAFP SACGKTNFAM LVPPAGFEGW
     SITTVGDDIA WIKPGADGKL YAINPEAGYF GVAPGTNMLT NPNCMLCLDK DVIYTNVALT
     DDGDVWWEGM EYDVPGKALP AHLIDWKGND WTPEIAKATG AKAAHPNSRF TVSALNNPAL
     DPEWDNPAGV PIDAFMFGGR RATTVPLVTE ARSWVEGVYM AATMGSETTA AAVGKSGVVR
     RDPFAMLPFT GYNMSDYFQH WLTLGAKLEA TGATLPKIYT TNWFRKGADG KFVWPGYGEN
     MRVLKWILDR LDGSAPEGVE HFFGVSPQYQ DLNWEGLAFT AEQFNTVISI DKAAWREEMV
     LHDELFEKLA YHMPQELIDK KARIKADIAA
//
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