ID   D6Z461_DESAT            Unreviewed;       971 AA.
AC   D6Z461;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=DaAHT2_1643 {ECO:0000313|EMBL:ADH86336.1};
OS   Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfobulbaceae; Desulfurivibrio.
OX   NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH86336.1, ECO:0000313|Proteomes:UP000001508};
RN   [1] {ECO:0000313|Proteomes:UP000001508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19089 / UNIQEM U267 / AHT2
RC   {ECO:0000313|Proteomes:UP000001508};
RG   US DOE Joint Genome Institute;
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., Muyzer G.,
RA   Woyke T.;
RT   "Complete sequence of Desulfurivibrio alkaliphilus AHT2.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001940; ADH86336.1; -; Genomic_DNA.
DR   RefSeq; WP_013163863.1; NC_014216.1.
DR   AlphaFoldDB; D6Z461; -.
DR   STRING; 589865.DaAHT2_1643; -.
DR   KEGG; dak:DaAHT2_1643; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_7; -.
DR   InParanoid; D6Z461; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001508; 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:ADH86336.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001508}.
FT   REGION          107..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        599
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   971 AA;  110029 MW;  13F7B09C54E58A1E CRC64;
     MEPGVFTSTL TGWQPEDSAT LAGQVGLLGR LLGRSIKELR GAAVLEQVED LRQLCKQAMV
     ENRPELRRQV AQRIADLDCR EIVHLLHAYT AFFHLVNKVE QMEITRVYRE PDPSPPPATP
     GENSRRRETI DAAVRGLKEQ GCSLQQTLAV LSRLDIQPTL TAHPTEARRR SILYKQKQVA
     SLLGRLRREA LTTDERDELL GEISNQIGLL LTTDDIRQTR PTVDDEVESG LYFVRNAIWA
     TVPRIYRDLR AALWRHYGES PEILPVLLRF RSWIGSDRDG NPNVTAAVSR RTYHYQRRVV
     LQLYLDELCE LRRELSLSSR QAPPSEALRN SLEEDGRTLA IDEQRRRHYR NEPYRLKITY
     IMARLRSLLW QMENRPRELA AGDYHCPAFL ADLQLLAASL RESGFSRLVS QGRLGRLLVR
     VRTFGFHLVA LDFRQHSQVH EETVALLLRL AGVEEDYLSL PEERRLALLQ EELGNPRPLL
     PRGCELPPEA RDLLETLALI GELQRLDPAS VGSYIISMTH QVSDLLEVLL LAKEAGIWRL
     RDGGVESRLQ LVPLFETIED LELSGRLVEK MLANPVYRQH LAAQNDFQEV MLGYSDSNKD
     GGYWMANWAL HRAQERLGQV CRQYGVDLRL FHGRGGTVGR GGGRSSQAIV AMPEVVHNGR
     IRFTEQGEVI SFRYAFADLA HRHLEQIFYA MIRTAGRVAR LAEQQAEPGA AGEAVEAAAD
     AEPGRLEGIE AGVAPERLQE FSALMDEVAQ RSMQAYRELV RDPEFWAWYT RVTPIEQISR
     LPIASRPVSR KAAGDVDLDG LRAIPWVFAW IQTRYIVPGW YGVGAALGEL SGTERGRQTL
     KQMYEQWPFF RMLIDNARRE MGRTRLEIAA DYAALANDLA VKDFHAQISR DFAEGRQALL
     ELSGEEELLG GSPEVQRSIA LRNPYTDVLN LLQVELLRRY HDSGGDEERE ALWDALFLSV
     NGIAAAMQST G
//