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
//