ID   A4YR74_BRASO            Unreviewed;       933 AA.
AC   A4YR74;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
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   ECO:0000313|EMBL:CAL76400.1};
GN   OrderedLocusNames=BRADO2580 {ECO:0000313|EMBL:CAL76400.1};
OS   Bradyrhizobium sp. (strain ORS 278).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL76400.1, ECO:0000313|Proteomes:UP000001994};
RN   [1] {ECO:0000313|EMBL:CAL76400.1, ECO:0000313|Proteomes:UP000001994}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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; CU234118; CAL76400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4YR74; -.
DR   STRING; 114615.BRADO2580; -.
DR   KEGG; bra:BRADO2580; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   Proteomes; UP000001994; 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:CAL76400.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001994}.
FT   ACT_SITE        166
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   933 AA;  104734 MW;  83C7572B3958730B CRC64;
     MLESVSMSPQ AITEEIRPNR AADVQAMEAD AQLREDIRLL GRILGDTVRD QEGADVFDLV
     ERIRQTSVRF HRDEDRQARR ELEQILDGMT IAETVRIVRA FSYFSHLANI AEDQNNIRRM
     RAKSDANGGA GMLAATLAHA KSAGFDAAEL RKFFSTALVS PVLTAHPTEV RRKSTMDREM
     EVAMLLDRRE RMQLTPEERE ANDEALRRAV LTLWQTNLLR RTKLTVLDEV TNGLSFYDYT
     FLREVPRLLC SLEDRLNDGA EVAGDLASFL RMGSWIGGDR DGNPFVTAEV MRGTLKLQSS
     LAMHYYLEEL HLLGSELSIA AHLADVSEEL RALAEKSPDT SPHRRGEPYR LAVSGIYARL
     AATAKKLGIE ISRLPVADVA PYDSVKELQD DLDVLHHSLI ANNAEVIARG RLRLLRRAVD
     CFGFHLARLD IRQNSAVHER TVAELIDTAM PGMSYLALSE DARVGLLVNE LRNTRPLVSH
     FVKYSDETIG ELELFRAAAE AHATFGADVI SQCIISMCKG MSDMLEVALL LKEVGLIDPS
     GRCAVNIVPL FETIEDLQAS SGIMDRMLAL HDYRRLVDSR GAVQEVMLGY SDSNKDGGFV
     TSGWELYKAE IHLVEIFERH HVRLRLFHGR GGSVGRGGGP SYDAIIAQPG GAVNGQIRIT
     EQGEIISSKY SNAEVGRYNL EILAAATLEA SLLHPRQPAP KREYLTAMDR LSELAFKAYR
     GLVYETDGFV DYFWSSTVIN EIATLNIGSR PASRKKTRAI EDLRAIPWVF SWAQCRLMLP
     GWYGFGSAVE AWIAENPEQG MPFLRELYQE WPFFRMLLSN MDMVLAKSSI AIASRYAELV
     PDEALREQIF GRIRREWNLV IETLLDITGQ ERLLQGNPLL ERSVRNRFPY LDPLNHVQVE
     LLKEHRAQNP DEQVLRGIQL TINGISAGLR NTG
//