ID   F2JTX8_MARM1            Unreviewed;       876 AA.
AC   F2JTX8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
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=Marme_1124 {ECO:0000313|EMBL:ADZ90399.1};
OS   Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS   MMB-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ90399.1, ECO:0000313|Proteomes:UP000001062};
RN   [1] {ECO:0000313|EMBL:ADZ90399.1, ECO:0000313|Proteomes:UP000001062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC   {ECO:0000313|Proteomes:UP000001062};
RX   PubMed=22675599; DOI=10.4056/sigs.2545743;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA   Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA   Sanchez-Amat A.;
RT   "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT   mediterranea type strain (MMB-1(T)).";
RL   Stand. Genomic Sci. 6:63-73(2012).
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; CP002583; ADZ90399.1; -; Genomic_DNA.
DR   RefSeq; WP_013660304.1; NZ_CP047696.1.
DR   AlphaFoldDB; F2JTX8; -.
DR   STRING; 717774.Marme_1124; -.
DR   KEGG; mme:Marme_1124; -.
DR   PATRIC; fig|717774.3.peg.1165; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001062; 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:ADZ90399.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001062}.
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   876 AA;  99204 MW;  70820DEC4FEEC66B CRC64;
     MSDRQASLRE NVRLLGDCLG ETMSNHLGDD FLQTVETIRQ LSKDGRQLGD SQALIKALEE
     LNDEDIVPVA RAFNQFLNLS NIAEQYHRVH RRKTNESLGV YKNPLGDLLT RLEEKQFSPE
     QMLETLKKQN IELVLTAHPT EIVRRSLIRK YDNISSELES LDKDNILPLE ESKHIRRLKE
     IITQAWHTDE IRAERPSPVD EAKWGYAVIE QSLWQAVPRF FRQLDEQFSR YTDSDHLPLD
     LSPIRFASWM GGDRDGNPNV THTVTEEVTL LARWMAADLY IKDLNLLRSE FSMTQCNDAL
     RDRVGDSVQP YREVLRNLEQ KMTRTKEWAQ ARLDGEEASS VGIILDSEDL LNDLTLCYQS
     LLDSGMKVIA NGSLLDLIRC AATFGVTLLK LDVRQDASRH IDAISAITRF YGLGDYAEWD
     EASRQAFLLA ELNSRRPLIP MEWEPNAEVQ EVLDSFAMIA RGHQNSFGSY VISMASAPSD
     VLAVALLLKE SKVSFPMRIV PLFETLADLD NAEPIIEQLL SIPWYKAYID GKQEVMIGYS
     DSAKDAGQIA ATWGQYRAQE ALTRLCEKHG VHLTLFHGRG GTVGRGGGPA HVAILSQPPG
     SVNGAIRVTE QGEMIRFKFG IPDIAVRSLE LYCSAVMEAT LMPAEAPKQE WRAIMDEIAE
     VGMNQYRSIV RGHEEFVPYF RAITPEQELA KLPLGSRPAR RRSDGGVESL RAIPWIFAWM
     QIRLMLPAWL GAESALQQAI DSGHLDKLRE MHENWPFFGA YLDMLDMVLA KSEPEIAEYY
     EKRLVTPELQ GLGQLLRNKL SQVSALVKQL KQQDRLIEDN KTIRQSIDVR NPYIDPLHYL
     QAELLYRSRK DDQNSAVDKA LMITMAGIAS GMQNTG
//