ID A9GNI8_SORC5 Unreviewed; 913 AA.
AC A9GNI8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
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:CAN93586.1};
GN OrderedLocusNames=sce3427 {ECO:0000313|EMBL:CAN93586.1};
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385 {ECO:0000313|EMBL:CAN93586.1, ECO:0000313|Proteomes:UP000002139};
RN [1] {ECO:0000313|EMBL:CAN93586.1, ECO:0000313|Proteomes:UP000002139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56 {ECO:0000313|Proteomes:UP000002139};
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(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|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; AM746676; CAN93586.1; -; Genomic_DNA.
DR RefSeq; WP_012236057.1; NC_010162.1.
DR AlphaFoldDB; A9GNI8; -.
DR STRING; 448385.sce3427; -.
DR KEGG; scl:sce3427; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_7; -.
DR OrthoDB; 9768133at2; -.
DR BioCyc; SCEL448385:SCE_RS17530-MONOMER; -.
DR Proteomes; UP000002139; 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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF00311; PEPcase; 2.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00781; PEPCASE_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000002139}.
FT REGION 362..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 579
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ SEQUENCE 913 AA; 100841 MW; 2C283AFA036E83AE CRC64;
MPPRRREVDR PLRKEVRLLG RLLGEVLIEQ EGEELFAIEE RIRTLAIRRR RGPSDGRAHA
AAELSKLLAE LPHDRLEPVI RAFTVYFRLV NLAEQHHRIR RARAYATDPG ARPQRGSIEA
AMHTLKKAGV PAERVRAALR TLDVTLTLTA HPTEAARRTV LEKLYRIAKN LEERDRCQLT
PDESARKLAE IREEITALWQ TDEVRRDRPT VGDEVKNVAW YIEEILWDLL PDLPTVIGRA
FEAAYGEPLD AEIAPLRIHS WVGADMDGNP LVVPAVLEDA LFAYRIRGLR RLVRAVRDLG
GALSQSVRHV TPPPWLLASI EEDAAAMPEV AAHFGPRTEG EPWRRKLHFI EARLTATLEH
AEHGRAEARA RSGQGPAREG RAFVRPEEPT LAVPYREPAE LERDLAVVAD SLRAARCASS
GERRARALLS QVRALGFALA ELEMRAPAED ARAAAASLAE GRVEPAQMTP EARRVFEALQ
RIAAAQRDGG ESSCRTLVLS MTHSEDDVLA ALASAKAAGL WDEARSCARI DVVPLFESLA
ALNDSARILR ALLAHPEYRP HVLARGVQEV MIGYSDSGKE VGLLAASAAL RRVQETLPKI
AAEAELPLRV FHGRGESVAR GGGPAHQALL ALPAGSVGGR YKATEQGEAL DHKYARPELA
MRTLEIMLSG VLLHTLGAQP RPPAASELRY AAAFDELAET GRRAYRALVW EEPKFVEFFT
AVTPIDEIAR LPLGSRPSKR RAGGLESLRA IPWVFAWTQN RAILPGWYGV GSGLEAMGQR
PEGAELLKEM MASWPFFRAV IDNVEMVLAK ADMTIFAGYA ELAPAAARKA VAPRIIAEYK
RTRSWLKRLT GNRRLLEGNP TLQRSISLRN PYVDPLSFLQ VELLRASRGG DSGRDRSLLL
TLNGIAAGMR NTG
//
