ID   J7SKH2_MORMO            Unreviewed;       877 AA.
AC   J7SKH2;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
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=MU9_593 {ECO:0000313|EMBL:AGG29639.1};
OS   Morganella morganii subsp. morganii KT.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG29639.1, ECO:0000313|Proteomes:UP000011834};
RN   [1] {ECO:0000313|EMBL:AGG29639.1, ECO:0000313|Proteomes:UP000011834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT {ECO:0000313|EMBL:AGG29639.1,
RC   ECO:0000313|Proteomes:UP000011834};
RX   PubMed=23282187;
RA   Chen Y.T., Peng H.L., Shia W.C., Hsu F.R., Ken C.F., Tsao Y.M., Chen C.H.,
RA   Liu C.E., Hsieh M.F., Chen H.C., Tang C.Y., Ku T.H.;
RT   "Whole-genome sequencing and identification of Morganella morganii KT
RT   pathogenicity-related genes.";
RL   BMC Genomics 13:S4-S4(2012).
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, ECO:0000256|HAMAP-
CC         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; CP004345; AGG29639.1; -; Genomic_DNA.
DR   RefSeq; WP_004236599.1; NC_020418.1.
DR   AlphaFoldDB; J7SKH2; -.
DR   GeneID; 69680473; -.
DR   KEGG; mmk:MU9_593; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000011834; 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:AGG29639.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011834}.
FT   ACT_SITE        137
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   877 AA;  98987 MW;  AC6E4CB063EFEFF7 CRC64;
     MNQQYSAMRS NVSMLGKLLG DTIKEAQGEH ILEKVESIRK LSKASQAGNE IQRQKLLMTL
     QNLSNEELLP VARAFNQFLN LTNVAEQYHS ISPHGEAASN PVALAALFDQ LKAKNFTNEE
     MRKAVDELSI ELVLTAHPTE IARRTLIHKL VAVNTCLAQL DHDDLADYEH DRIMRRLRQL
     VAQAWHTDEI RKDRPTPLDE AKWGFAVVEN SLWEGVPAFL REFNEQLEAS LDYNLSVEAT
     PIRFTSWMGG DRDGNPNVTA DITRRVLTLS RWKAADLFYN DIQVLVSELS MSECTPELRE
     RVGEDAAEPY RVITKQLRAR LKSTLDYLER CLAGEPAIKP DNLLTDNEEL WEPLYLCYRS
     LVECGMKIIA NGQLLDTLRR IRCFGLQLVR IDVRQESTRH TEALSELTQY LGLGDYAAWP
     EEEKQEFLLR ELQSKRPLVP QNWECSNETR EVFDTCRVIA ESPENSVASY VISMAKVPSD
     VLAVKLLLKE SGSPVTLPVA PLFETLDDLN NAESVITRLL SIDWYRNLIN DRQMVMIGYS
     DSAKDAGVMA ASWAQYRAQD ALIKVCAREG VTLTLFHGRG GTIGRGGAPA HAALLSQPPG
     SLKGGLRVTE QGEMIRFKFG LPQVTISSLA MYASASLEAN LLPPPEPKPE WAAIMDRLSD
     ISCEMYRDYV REQPDFVPYF RAATPEQELG KLPLGSRPAK RRPTGGVETL RAIPWIFAWS
     QNRLMLPAWL GAGAALKTAV DEGNRAMLEV MYYQWPFFRT RIGMLEMVFA KVDLWLAEYY
     DQRLVEPRLW PLGAKLREQL SQDIKSVLMI SKDEQLMADL PWIAESIALR NVYTDPLNVL
     QAELLHRSRE CDQSDPQVEQ ALMVTIAGIA AGMRNTG
//