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Entry: A0A1T0AUZ2_9PAST
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Original site: A0A1T0AUZ2_9PAST 
ID   A0A1T0AUZ2_9PAST        Unreviewed;       536 AA.
AC   A0A1T0AUZ2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000256|ARBA:ARBA00012363, ECO:0000256|HAMAP-Rule:MF_00453};
DE            Short=PCK {ECO:0000256|HAMAP-Rule:MF_00453};
DE            Short=PEP carboxykinase {ECO:0000256|HAMAP-Rule:MF_00453};
DE            Short=PEPCK {ECO:0000256|HAMAP-Rule:MF_00453};
DE            EC=4.1.1.49 {ECO:0000256|ARBA:ARBA00012363, ECO:0000256|HAMAP-Rule:MF_00453};
GN   Name=pckA {ECO:0000256|HAMAP-Rule:MF_00453};
GN   ORFNames=B0187_01080 {ECO:0000313|EMBL:OOS00529.1};
OS   Haemophilus paracuniculus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=734 {ECO:0000313|EMBL:OOS00529.1, ECO:0000313|Proteomes:UP000190867};
RN   [1] {ECO:0000313|EMBL:OOS00529.1, ECO:0000313|Proteomes:UP000190867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 43573 {ECO:0000313|EMBL:OOS00529.1,
RC   ECO:0000313|Proteomes:UP000190867};
RA   Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA   Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT   "Draft genome sequence of Haemophilus paracuniculus CCUG 43573 type
RT   strain.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of
CC       oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct
CC       phosphoryl transfer between the nucleoside triphosphate and OAA.
CC       {ECO:0000256|HAMAP-Rule:MF_00453}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:18617, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC         EC=4.1.1.49; Evidence={ECO:0000256|ARBA:ARBA00001389,
CC         ECO:0000256|HAMAP-Rule:MF_00453};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00453};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00453};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|HAMAP-Rule:MF_00453}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00453}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00453}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC       family. {ECO:0000256|ARBA:ARBA00006052, ECO:0000256|HAMAP-
CC       Rule:MF_00453}.
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:OOS00529.1}.
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DR   EMBL; MUYA01000002; OOS00529.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T0AUZ2; -.
DR   STRING; 734.B0187_01080; -.
DR   OrthoDB; 9806325at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000190867; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP 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:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00484; PEPCK_ATP; 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_00453; PEPCK_ATP; 1.
DR   InterPro; IPR001272; PEP_carboxykinase_ATP.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   InterPro; IPR015994; PEPCK_ATP_CS.
DR   NCBIfam; TIGR00224; pckA; 1.
DR   PANTHER; PTHR30031:SF0; PHOSPHOENOLPYRUVATE CARBOXYKINASE (ATP); 1.
DR   PANTHER; PTHR30031; PHOSPHOENOLPYRUVATE CARBOXYKINASE ATP; 1.
DR   Pfam; PF01293; PEPCK_ATP; 1.
DR   PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR   SUPFAM; SSF68923; PEP carboxykinase N-terminal domain; 1.
DR   SUPFAM; SSF53795; PEP carboxykinase-like; 1.
DR   PROSITE; PS00532; PEPCK_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00453}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00453}; Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Kinase {ECO:0000313|EMBL:OOS00529.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00453};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00453};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00453}; Pyruvate {ECO:0000313|EMBL:OOS00529.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190867};
KW   Transferase {ECO:0000313|EMBL:OOS00529.1}.
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         209
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         209
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         228
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         244..252
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         265
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         293
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         329
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         445..446
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
FT   BINDING         451
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00453"
SQ   SEQUENCE   536 AA;  59149 MW;  FD5C32E562CC4868 CRC64;
     MLNRVERELA ELGITNVKEI VHNPSYEQLF EEETKPELEG FEKGRLTTSG AVAVDTGIFT
     GRSPKDKFIV LDEKTKDTVW WTSEAVKNDN KPMNQATWQS LKDLVTKQLS NKRLFVIDAF
     CGANKDSRLA VRIVTEVAWQ AHFVKNMFIR PSQAELQDFK PDFVVMNGSK CTNPNWKEQG
     LNSENFVAFN ITEGIQLIGG TWYGGEMKKG MFSMMNYLLP LKGIASMHCS ANVGEQGDVA
     VFFGLSGTGK TTLSTDPKRK LIGDDEHGWD DDGVFNYEGG CYAKTINLSP ENEPDIYGAI
     KRDALLENVV VREDGSIDFA DGSKTENTRV SYPIYHINNI VEPVSKAGHA KKVIFLTADA
     FGVLPPVSKL TPEQTKYYFL SGFTAKLAGT ERGITEPTPT FSACFGAAFL SLHPTQYAEV
     LVKRMEASGA EAYLVNTGWN GSGKRISIKD TRGIIDAILD GSIEKSETKQ LPIFDLAVPT
     SLPNVDPAIL DPRDTYADPA QWQTKAEDLA QRFVKNFEKY TTNAEGKALV AAGPKA
//
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