ID   F4GRT5_PUSST            Unreviewed;       950 AA.
AC   F4GRT5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
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=PT7_3476 {ECO:0000313|EMBL:AEC22016.1};
OS   Pusillimonas sp. (strain T7-7).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pusillimonas.
OX   NCBI_TaxID=1007105 {ECO:0000313|EMBL:AEC22016.1, ECO:0000313|Proteomes:UP000008737};
RN   [1] {ECO:0000313|EMBL:AEC22016.1, ECO:0000313|Proteomes:UP000008737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T7-7 {ECO:0000313|EMBL:AEC22016.1,
RC   ECO:0000313|Proteomes:UP000008737};
RX   PubMed=21622753; DOI=10.1128/JB.05242-11;
RA   Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.;
RT   "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant diesel
RT   oil-degrading bacterium isolated from the Bohai Sea in China.";
RL   J. Bacteriol. 193:4021-4022(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T7-7;
RA   Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.;
RT   "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7-7, a
RT   novel species isolated from the Bohai Sea, China.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002663; AEC22016.1; -; Genomic_DNA.
DR   RefSeq; WP_013744533.1; NC_015458.1.
DR   AlphaFoldDB; F4GRT5; -.
DR   STRING; 1007105.PT7_3476; -.
DR   KEGG; put:PT7_3476; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008737; 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:AEC22016.1}.
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        595
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   950 AA;  106520 MW;  B9FEB6B3BFCABD2E CRC64;
     MNQPDAASTE STFLRNNIRQ LGKTLGEVIK ECEGKAAYDV IEKLRRAAVK FRREGNPADS
     RVLEQQIAKL PDEEANSVAR AFSYFLHLSN IAEDRDQNRR QRHHELHADT PMRGSLQHAL
     DLLHSKGVGS RKILRYLESA CIVPVLTAHP TEVQRKSTLD LHREIARQLA QSDANLTPSE
     RKLLDQTLTG LVATLWQTRM LRRQKLTVLD EIDNALTYYT STFLTAIPRL YQDLATRLRP
     ERKHFDIKTR PLPPFLQMGS WIGGDRDGNP NVDASTLEQA LLRQSTHVLR HYLQEIKTLG
     TELSLSRTLG TASPELLALS LVSQDNSAHR VDEPYRRAFI HLYARLAATS VALAERQLAL
     RPTYDAPPYE TPADFQHDLQ IIADSLDQHH GSLIAQLRLS GLLQAVSIFG FHLASVDLRQ
     SSDVHERVLT ELFKAAGVRL NNKPVNYSAL SEEDRISLLR EEVRQIRPLA SPWISYTPET
     EKELAILRMA AACRRKYGAA AIRQSIVSHT ETLSDLLEVL VLQQETGLIA PDAGKASHQG
     ADGLMVVPLF ETIPDLMRGP QIMDDWLGLP EVAKRIQNTH DGVQEVMLGY SDSNKDGGYL
     TSNWSLYYAE RQLVQVFKKR KVRLRLFHGR GGSVARGGGP SFDAIQAQPP GTVNGQIRLT
     EQGEVIQGKY KDSEVGRWHL ENFVAAVLET SLATGPSASQ TEDKNMSRFG SAMDTMSDAA
     QQSYRDLVYG TPGFNDYFFA STPILEIAGL NIGSRPASRK SSQKIEDLRA IPWGFSWAQC
     RLMLTGWYGM GTALHNYIEN GSAGAPATPE LRLAQLQEMA DIWPFFRTLL SNMEQVLAKT
     DLGIARRYAS LVPDKKLRKH VFGRIEAEFD LTLDMFRKIS RHELLAKDEL LGAALSERFA
     YIDPLNHLQV ELLQRHRQAH ESQSDDEESR SQRAIHMTIN GIAAGLRNSG
//