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
//