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Database: UniProt/TrEMBL
Entry: A0A0E1CR29_KLEPN
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ID   A0A0E1CR29_KLEPN        Unreviewed;       891 AA.
AC   A0A0E1CR29;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=KPNJ1_05351 {ECO:0000313|EMBL:AHM87739.1};
OS   Klebsiella pneumoniae 30660/NJST258_1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1420012 {ECO:0000313|EMBL:AHM87739.1, ECO:0000313|Proteomes:UP000019583};
RN   [1] {ECO:0000313|EMBL:AHM87739.1, ECO:0000313|Proteomes:UP000019583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=30660/NJST258_1 {ECO:0000313|EMBL:AHM87739.1,
RC   ECO:0000313|Proteomes:UP000019583};
RX   PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA   Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA   Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J., Bonomo R.A.,
RA   Musser J.M., Kreiswirth B.N.;
RT   "Molecular dissection of the evolution of carbapenem-resistant multilocus
RT   sequence type 258 Klebsiella pneumoniae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(2014).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP006923; AHM87739.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E1CR29; -.
DR   KEGG; kpa:KPNJ1_05351; -.
DR   PATRIC; fig|1420012.3.peg.4987; -.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000019583; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:AHM87739.1}.
FT   ACT_SITE        146
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        554
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   891 AA;  99960 MW;  3C6B26DB91B74046 CRC64;
     MRWGVWGNMN EQYSALRSNV SMLGKVLGDT IKDALGENIL DRVETIRKLS KSSRAGNEAN
     RQELLTTLQN LSNDELLPVA RAFSQFLNLA NTAEQYHSIS PNGEAASNPE VIARTLRKLK
     DQPNLNEETI KKAVESLSLE LVLTAHPTEI TRRTLIHKMV EVNNCLKQLD NKDIADYEHH
     QLMRRLRQLI AQSWHTDEIR KHRPSPVDEA KWGFAVVENS LWEGVPNYLR ELNEQLEANL
     GYQLPVDFVP VRFTSWMGGD RDGNPNVTAD ITRHVLLLSR WKATDLFLKD VQVLISELSM
     VECTDELRAL AGAEGAQEPY RYLMKKLRSQ LMETQAWLEA RLKGQKLPKP AGLITQNEQL
     WEPLYACYKS LQACGMGIIA NGELLDTLRR VKSFGVPLVR IDIRQESTRH TEALGEMTRY
     LGIGDYESWS EADKQAFLIR ELNSKRPLLP RQWEPSEETR EVLDTCKVIA EAPRGSIAAY
     VISMAKTPSD VLAVHLLLKE AGIGFALPVA PLFETLDDLN NANDVMTQLL NIDWYRGFIQ
     GKQMVMIGYS DSAKDAGVMA ASWAQYQAQD ALIKTCEKAG IELTLFHGRG GSIGRGGAPA
     HAALLSQPPG SLKGGLRVTE QGEMIRFKYG LPEVTISSLS LYTSAILEAN LLPPPEPKAE
     WRDIMAELSD VSCKMYRGYV RENKDFVPYF RSATPEQELG KLPLGSRPAK RRPTGGVESL
     RAIPWIFAWT QNRLMLPAWL GAGAALQKVV EGGKQSELEA MCRDWPFFST RLGMLEMVYS
     KADLWLAEYY DQRLVKPELW ALGSELRKLL AADINVVLAI ANDSHLMADL PWIAESIQLR
     NIYTDPLNVL QAELLHRSRQ AEEEGKDPDP RVEQALMVTI AGVAAGMRNT G
//
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