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PCKA_BACTN
ID   PCKA_BACTN              Reviewed;         535 AA.
AC   Q8A414;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase (ATP) {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PEP carboxykinase {ECO:0000255|HAMAP-Rule:MF_00453};
DE            Short=PEPCK {ECO:0000255|HAMAP-Rule:MF_00453};
DE            EC=4.1.1.49 {ECO:0000255|HAMAP-Rule:MF_00453};
GN   Name=pckA {ECO:0000255|HAMAP-Rule:MF_00453}; OrderedLocusNames=BT_2790;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_00453};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00453};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00453};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00453}.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase (ATP)
CC       family. {ECO:0000255|HAMAP-Rule:MF_00453}.
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DR   EMBL; AE015928; AAO77896.1; -; Genomic_DNA.
DR   RefSeq; NP_811702.1; NC_004663.1.
DR   RefSeq; WP_008761973.1; NZ_UYXG01000001.1.
DR   AlphaFoldDB; Q8A414; -.
DR   SMR; Q8A414; -.
DR   STRING; 226186.BT_2790; -.
DR   PaxDb; Q8A414; -.
DR   PRIDE; Q8A414; -.
DR   EnsemblBacteria; AAO77896; AAO77896; BT_2790.
DR   GeneID; 60923969; -.
DR   KEGG; bth:BT_2790; -.
DR   PATRIC; fig|226186.12.peg.2837; -.
DR   eggNOG; COG1866; Bacteria.
DR   HOGENOM; CLU_018247_0_1_10; -.
DR   InParanoid; Q8A414; -.
DR   OMA; MRYAGEM; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004612; F:phosphoenolpyruvate carboxykinase (ATP) activity; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   CDD; cd00484; PEPCK_ATP; 1.
DR   Gene3D; 3.40.449.10; -; 1.
DR   Gene3D; 3.90.228.20; -; 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   PANTHER; PTHR30031; PTHR30031; 1.
DR   Pfam; PF01293; PEPCK_ATP; 1.
DR   PIRSF; PIRSF006294; PEP_crbxkin; 1.
DR   SUPFAM; SSF68923; SSF68923; 1.
DR   TIGRFAMs; TIGR00224; pckA; 1.
DR   PROSITE; PS00532; PEPCK_ATP; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Decarboxylase; Gluconeogenesis; Lyase; Manganese;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..535
FT                   /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT                   /id="PRO_0000203811"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         207
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         207
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         226
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         226
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         243..251
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         264
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         328
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         328
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         444..445
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         450
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
SQ   SEQUENCE   535 AA;  59163 MW;  C626BE8D2BB4DB4E CRC64;
     MANLDLSKYG ITGVTEIVHN PSYDVLFAEE TKPGLEGFEK GQVTNMGAVN VMTGVYTGRS
     PKDKFFVKDE TSENTVWWTS EEYKNDNKPV DAKCWAAVKD LATKELSNKR LFVVDAFCGA
     NENSRLKLRF IMEVAWQAHF VTNMFIRPTA EELANFGEPD FVIMNASKAK VENYKELGLN
     SETAVVFNLT EKIQVILNTW YGGEMKKGMF SYMNYLLPLN GMASMHCSAN TDKEGKSSAI
     FFGLSGTGKT TLSTDPKRLL IGDDEHGWDD EGVFNFEGGC YAKVINLDKE SEPDIWNAIK
     RDALLENCTV NAEGEINFAD KSVTENTRVS YPIYHIENIV KPVSKGPHAK QVIFLSADAF
     GVLPPVSILN AEQTKYYFLS GFTAKLAGTE RGITEPTPTF SACFGAAFLS LHPTKYGEEL
     VKKMEKTGAK AYLVNTGWNG TGKRISIKDT RGIIDAILDG SIDKAPTKVM PYFDFVVPTE
     LPGVDPKILD PRDTYECACQ WEEKAKDLAG RFIKNFAKFT GNEAGKALVA AGPKL
 
 
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