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Database: UniProt/TrEMBL
Entry: M4ZC32_9BRAD
LinkDB: M4ZC32_9BRAD
Original site: M4ZC32_9BRAD 
ID   M4ZC32_9BRAD            Unreviewed;       928 AA.
AC   M4ZC32;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=S58_50320 {ECO:0000313|EMBL:BAM91011.1};
OS   Bradyrhizobium oligotrophicum S58.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1245469 {ECO:0000313|EMBL:BAM91011.1, ECO:0000313|Proteomes:UP000011841};
RN   [1] {ECO:0000313|EMBL:BAM91011.1, ECO:0000313|Proteomes:UP000011841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S58 {ECO:0000313|EMBL:BAM91011.1,
RC   ECO:0000313|Proteomes:UP000011841};
RX   PubMed=23396330; DOI=10.1128/AEM.00009-13;
RA   Okubo T., Fukushima S., Itakura M., Oshima K., Longtonglang A.,
RA   Teaumroong N., Mitsui H., Hattori M., Hattori R., Hattori T.,
RA   Minamisawa K.;
RT   "Genome analysis suggests that the soil oligotrophic bacterium Agromonas
RT   oligotrophica (Bradyrhizobium oligotrophicum) is a nitrogen-fixing symbiont
RT   of Aeschynomene indica.";
RL   Appl. Environ. Microbiol. 79:2542-2551(2013).
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,
CC         ECO:0000256|HAMAP-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; AP012603; BAM91011.1; -; Genomic_DNA.
DR   RefSeq; WP_015668100.1; NC_020453.1.
DR   AlphaFoldDB; M4ZC32; -.
DR   STRING; 1245469.S58_50320; -.
DR   KEGG; aol:S58_50320; -.
DR   PATRIC; fig|1245469.3.peg.5147; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000011841; 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:BAM91011.1}.
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        161
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        590
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   928 AA;  103919 MW;  EDA06FBF55F344A2 CRC64;
     MSPQIMPSED TRPNRAAEAQ AMEEDARLRD DIRLLGRILG DTVRDQEGAD VFDLVERIRQ
     TSVRFHRDED RQARHELEHI LDGMTTAETV RIVRAFSYFS HLANIAEDQN NIRRMRAKSD
     ANGGAGMLAS TLAHAKSAGF EAADLRKFFS TALVSPVLTA HPTEVRRKST MDREMEVAML
     LDRRERMQLT PDEREANDEA LRRAVLTLWQ TNLLRRTKLT VLDEVTNGLS FYDYTFLREV
     PRLLCALEDR LNDGAEVAGD LASFLRMGSW IGGDRDGNPF VTAEVMRGTL KLQSSLALHY
     YLEELHLLGG ELSMAAHLAD VSEELRALAE RSPDTSPHRI GEPYRLAVSG IYARLAATAK
     KLGIQISRLP VGAVAPYDSV KEFQDDLDVL HRSLIANNAE VIARGRLRLL RRAIDCFGFH
     LARLDIRQNS AVHERTVAEL IDTAMPGMSY LALSEDARVG LLVSELRNTR PLVSQFIKYS
     DETVGELALF RAAADAHATF GADVISQCII SMCKGMSDML EVALLLKEVG LIDPSGRCGV
     NIVPLFETIE DLQASSGIMD RMLALHDYRR LVDSRGAVQE VMLGYSDSNK DGGFVTSGWE
     LYKAEIGLVD IFERHGVRLR LFHGRGGSVG RGGGPSYDAI IAQPGGAVNG QIRITEQGEI
     ISSKYSNAEV GRNNLDILAA ATLEASLLHP RQPAPKREYL TAMDRLSELA FKAYRGLVYE
     TDGFVEYFWS STVINEIATL NIGSRPASRK KTRAIEDLRA IPWVFSWAQC RLMLPGWYGF
     GSAVESWIAE NPEQGMPFLR ELYREWPFFR MLLSNMDMVL AKSSIAIASR YAELVPDEAL
     REKIFGRIRR EWNLVIETLL DIMGQERLLQ GNPLLERSVR NRFPYLDPLN HVQVELLKEH
     RAQNPDEQVL RGIQLTINGI SAGLRNTG
//
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