ID   D5SQR0_PLAL2            Unreviewed;       915 AA.
AC   D5SQR0;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
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   OrderedLocusNames=Plim_2699 {ECO:0000313|EMBL:ADG68522.1};
OS   Planctopirus limnophila (strain ATCC 43296 / DSM 3776 / IFAM 1008 / Mu 290)
OS   (Planctomyces limnophilus).
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctopirus.
OX   NCBI_TaxID=521674 {ECO:0000313|EMBL:ADG68522.1, ECO:0000313|Proteomes:UP000002220};
RN   [1] {ECO:0000313|EMBL:ADG68522.1, ECO:0000313|Proteomes:UP000002220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43296 / DSM 3776 / IFAM 1008 / 290
RC   {ECO:0000313|Proteomes:UP000002220};
RX   PubMed=21304691; DOI=10.4056/sigs.1052813;
RA   Labutti K., Sikorski J., Schneider S., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Tindall B.J., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Planctomyces limnophilus type strain (Mu
RT   290).";
RL   Stand. Genomic Sci. 3:47-56(2010).
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; CP001744; ADG68522.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5SQR0; -.
DR   STRING; 521674.Plim_2699; -.
DR   KEGG; plm:Plim_2699; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_0; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002220; 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:ADG68522.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002220}.
FT   ACT_SITE        142
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        577
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   915 AA;  103268 MW;  275B7B9175529562 CRC64;
     MSAKPILSSD VETLTSLLGG AIVEQAGSDL AALLMRIRQL SRERRVGLPG AAERLVELLA
     GLNEDQLDLL TKSLSIYFDL ANVAEDLQRI RVIRQRERQS EGSVRKESLG DAIAQLKKQG
     ATAEAVQHLL DKLHIGLVFT AHPTEAKRRT TRRILRQLRS DLTTAHQGDL LPRESGVLQE
     RIRGSLTLLW QIDPMRPQPP TVMQEVERGL FFFDGLWDIV PLIFQDLRSA LAEHYPGFKF
     HVPPFLKFGS WIGGDRDGNP FVTAQVTSDT LRLLETTAIE RHLKTTRELA DLLVVSDRGM
     QPDDPVYAAL QKTFGAHPEL DQLVGDAPEA EPYRRWIKVI ELKLRKRIEP ALASPLKAYQ
     TAAELEADAR LIEESLLRRK GDRIHASFLA AWLDQIRTFG LQVSALDVRQ DSRVHVDVLQ
     EVFARAGIYA EYAKADEKTR QKILTTPHDL GMNVLEGELS DMARETFSLY KLMAETVRAG
     GIERFGGHIV SMTHYASDIL VILWFWKWAW KVTAGESKAE LPHLPLMPLL ETIDDLRQGP
     AILTDLLSVP DYLAYLKKDQ GAQPLQNVMV GYSDSTKDGG YLAASWGLYR AQEQLSDVLA
     SQGVRLRVFH GRGGALGRGG GPAARAILSL PPKSVDGSLR VTEQGEVLAE RYDEPQIAFR
     HLEQVTWATL LVSSTQEGHW PEDWFTHLDE LAQQSYLHYR KLVDDPGFLM YFDRATPISE
     IERLPIGSRP ARRRERKSLS DLRAIPWTFA WTQSRHMIPA WFGLGKALHD AVARNNEDWS
     RYQEMYRTWP IFQAIIDNAT LALMKADLQI ANRYADLVED REVAKRLWSM IHEEYDRSRA
     SVLMITGESS LLSNTPWLQT SIQERNPYVD PLNLIQVELL KRAREGSIEA DRAARLQHSV
     RLTIQGVAAG LRTTG
//