ID   I1XMT7_METNJ            Unreviewed;       947 AA.
AC   I1XMT7;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, 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=Q7A_2929 {ECO:0000313|EMBL:AFI85706.1};
OS   Methylophaga nitratireducenticrescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI85706.1, ECO:0000313|Proteomes:UP000009144};
RN   [1] {ECO:0000313|EMBL:AFI85706.1, ECO:0000313|Proteomes:UP000009144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI85706.1,
RC   ECO:0000313|Proteomes:UP000009144};
RX   PubMed=22815445; DOI=10.1128/JB.00726-12;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT   sp. strain JAM7.";
RL   J. Bacteriol. 194:4126-4127(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; CP003390; AFI85706.1; -; Genomic_DNA.
DR   RefSeq; WP_014708067.1; NC_017857.3.
DR   AlphaFoldDB; I1XMT7; -.
DR   STRING; 754476.Q7A_2929; -.
DR   KEGG; mej:Q7A_2929; -.
DR   PATRIC; fig|754476.3.peg.2875; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000009144; 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:SF46; 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}.
FT   ACT_SITE        157
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        604
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   947 AA;  108367 MW;  F3DAB50A08E4EF0E CRC64;
     MTTRQVDFSS AVALELLTDK DLRSHVRFLV NLLGEVIAEQ SGPEVYQVIE QLRKGFIRLR
     KEDDVELRQT LKDKIESLDE LTLREVIRAF NLYFSLVNTA EEAYHHHNRQ IQLRNGGNLW
     HGSFLDTLTQ FKNEGVLVKQ LQDLLEKLVF MPVFTAHPTE SKRRTVMEML RRVFLLDEKL
     TEGLITPFDQ QQIRNQLKRQ IQLLWSTDEV RAVKPSVRDE IKNGLYYFNV SLFDAVPRTY
     RNFENALRRV YGDELDPETP IVVPDYLRFG SWIGGDRDGN PFVTAQTTEM AIALQKRTVI
     RRYLEDVTKL SFILTQSQPL CEINTDLATD IEQSEQRFAG AFSTNPQRFI NEPYRRKLYM
     MRYRLKDNLA VLEEFFRPDL QIESLGVAYH NEDEFLADLY LIHKSLVDNG DIAIAAAELT
     DLIRLVKTFG FYLYNLDIRQ ESSKHTDAVG EILALTGLNR HYLQMDEAER QTLLTDLLAA
     PRLPEIYGDL QPDSLEILNV FRLIARLRVE VSEKAFGNYV ISMTHQASHI LEVMLLARFA
     DLIGQDEHGW FCHIRVAPLF ETIEDLEHIE PVMSALLENS QYRTLLSTSG NMQEVMLGYS
     DSCKDGGILA SAWNLYQAQK TVSRLSEQYA IGCRMFHGRG GTIGRGGGPT HDAILAQPVD
     TVHGQIKFTE QGEVLSFKYG NTETAAYELG MGVSALIKAS RGLVTDSAQE KPEYLSIMQQ
     LAQLGEQQYR QLTEQTPGFL DYFYEACPIS EIGLMNIGSR PSHRKIADRS KSSVRAIGWV
     FAWAQSRHTL PGWYGVGSAI ATWISDDPER RQILQKMYFE WPFFRAMVSN TQMSLSKADM
     DIAAEYADLC IDKLQAQQVL SVIRTEYQQT ASQLLQLTGA ETLMAENPQL ALSLRRRQAY
     LDPLNHIQLL LLKRYRHGDY SDAETAKWRD PLLRSISAIS QGMRNTG
//