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Database: UniProt
Entry: W0DYM6_MARPU
LinkDB: W0DYM6_MARPU
Original site: W0DYM6_MARPU 
ID   W0DYM6_MARPU            Unreviewed;       928 AA.
AC   W0DYM6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=MARPU_07305 {ECO:0000313|EMBL:AHF03690.1};
OS   Marichromatium purpuratum 984.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Marichromatium.
OX   NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF03690.1, ECO:0000313|Proteomes:UP000005275};
RN   [1] {ECO:0000313|EMBL:AHF03690.1, ECO:0000313|Proteomes:UP000005275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=984 {ECO:0000313|EMBL:AHF03690.1,
RC   ECO:0000313|Proteomes:UP000005275};
RG   DOE Joint Genome Institute;
RA   Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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,
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; CP007031; AHF03690.1; -; Genomic_DNA.
DR   RefSeq; WP_005223784.1; NZ_CP007031.1.
DR   AlphaFoldDB; W0DYM6; -.
DR   STRING; 765910.MARPU_07305; -.
DR   KEGG; mpur:MARPU_07305; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000005275; 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:SF46; 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:AHF03690.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005275}.
FT   ACT_SITE        145
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        587
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   928 AA;  104499 MW;  6C00CE204C706E12 CRC64;
     MNETVDDPVL EHDIELFTRL LGDVLREHSR KRVLVVVERL REGFMQLREG EDETLRARLR
     ARIEGLDPQT LAEVIRAFAI YFGLVNTAEE LNAHLQRMAR VSSGERLWRG SFDDTVRRLA
     ADGVAPAPFQ SLLEHLVYLP VFTAHPTEAR RRTIAEIFRR IFLAGQDLHR HRLNDEERED
     KLAEIRAQIQ ILWKTDEVRV HKPQVTDEVR QGLYFFRESL FGAVPEVYRI LEKAVRRVHG
     AATAAAVPSL MRFGSWIGGD RDGNPFVCPE TTELAVRMHA ELALEHYLER VGRLQRMLSH
     SSALCEPAPA FLDSLDADED YWVETMGQSL RRFLNEPYRR KLAMVAHRLE ANLARVRARL
     AEAETLPAAG YCDARAFLVD LRLIRDSLIH HGDASAAAGP LHDLIRLVET FGFHLVQLDL
     RQESSRHTEA VAELFARQPG APYYLAFDES QRLLALVEAI VHPQPFVIDK ATLGAATRET
     LETFETIARA RAEVGEQAIG QYVISMTHEA SHVLEVMLLA RLAGLAGRDR QGWFCTLQIA
     PLFETIDDLA RIDAVMGRLF TDPTYRALLR ASGDQQEVML GYSDSCKDGG ILASGWRLYE
     AQRKVIALAD EHGVACRLFH GRGGTVGRGG GPTHEAILAQ PADTVHGQIK FTEQGEVLSY
     RYANPETARY ELTMGISGLI KASRCLIESA APERAEDLEV MAELAAHGEA AYRALVGTEG
     LLDYFYACTP VDGIALLNIG SRPAHRSRGD RSLSSIRAIP WVFGWGQARL TLPGWFGIGT
     ALARYRGDDP ERLVRLRRMY GEWPFFRVLL SNTQMSLFKA EMAIAREYLR LADDPPRAAA
     LLAHIEAEYR LTLSEVLAVT ETDRLLADQP ALRRSLLRRN RYLDPLNHIQ VVLLERYRGE
     PEAEQREQWL DPLLRSINAI AAGMRNTG
//
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