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Database: UniProt
Entry: PCKA_LEPIC
LinkDB: PCKA_LEPIC
Original site: PCKA_LEPIC 
ID   PCKA_LEPIC              Reviewed;         530 AA.
AC   Q72VT0;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 105.
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=LIC_10216;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS68844.1; -; Genomic_DNA.
DR   RefSeq; WP_001148872.1; NC_005823.1.
DR   AlphaFoldDB; Q72VT0; -.
DR   SMR; Q72VT0; -.
DR   GeneID; 61143574; -.
DR   KEGG; lic:LIC_10216; -.
DR   HOGENOM; CLU_018247_0_1_12; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000007037; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
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; Cytoplasm; Decarboxylase; Gluconeogenesis; Lyase; Manganese;
KW   Metal-binding; Nucleotide-binding.
FT   CHAIN           1..530
FT                   /note="Phosphoenolpyruvate carboxykinase (ATP)"
FT                   /id="PRO_0000203825"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         193
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         199
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         199
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         218
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         234..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         255
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         320
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         320
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
FT   BINDING         445
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00453"
SQ   SEQUENCE   530 AA;  59174 MW;  CD908F94B7FB7C98 CRC64;
     MQAQTQVKGL KELGLEPSEI FHNLSYDEIY EHEKKNGETV VSSNGTMMVD TGIFTGRSPK
     DKYFVDEPSS NGNIWWSHIN FKVSEAIFDE LYKKCVNYLS HKKLYVFDGY AGANPETRVS
     LRVVSEKAWQ HHFCTNMFLR PTKEELVGLD PEFTIINACG IKNENFKQHG MNSEVFVIFH
     LAKKICIIGG TEYGGEMKKG IFSVMNYKLP LQGILSMHCS ANVGQDGDTA LFFGLSGTGK
     TTLSTDPNRK LIGDDEHGWD DNGIFNIEGG CYAKVINLDP KTEPDIYEAI RKDALLENVV
     YDPQTKIVDY SSAAKTENTR VSYPIFHINN IQVPSKGGHP KTIIFLTYDA FGVLPPVSKL
     SIEQAMYHFL SGYTAKVAGT ERGIKEPTAT FSACFGAAFM TLHPTKYAKL LGEKMKKHNV
     RAYLMNTGLV GGSYGVGKRM NLPSTRKIID EILNGNIEKS EFVTHPVFQV AYPKTISGVD
     SAILDPREAW TDKAAYDQTA KKLGEMFIKN FKQYAEGSKD FDFTAFGPKI
//
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