ID   Q4FMJ1_PELUB            Unreviewed;       895 AA.
AC   Q4FMJ1;
DT   30-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
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:AAZ21598.1};
GN   OrderedLocusNames=SAR11_0780 {ECO:0000313|EMBL:AAZ21598.1};
OS   Pelagibacter ubique (strain HTCC1062).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae; Pelagibacter.
OX   NCBI_TaxID=335992 {ECO:0000313|EMBL:AAZ21598.1, ECO:0000313|Proteomes:UP000002528};
RN   [1] {ECO:0000313|EMBL:AAZ21598.1, ECO:0000313|Proteomes:UP000002528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC1062 {ECO:0000313|EMBL:AAZ21598.1,
RC   ECO:0000313|Proteomes:UP000002528};
RX   PubMed=16109880; DOI=10.1126/science.1114057;
RA   Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA   Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA   Carrington J.C., Mathur E.J.;
RT   "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL   Science 309:1242-1245(2005).
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; CP000084; AAZ21598.1; -; Genomic_DNA.
DR   RefSeq; WP_011281937.1; NC_007205.1.
DR   AlphaFoldDB; Q4FMJ1; -.
DR   STRING; 335992.SAR11_0780; -.
DR   KEGG; pub:SAR11_0780; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_1_0_5; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002528; 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:AAZ21598.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002528}.
FT   ACT_SITE        154
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        560
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   895 AA;  103510 MW;  4C20FDD8DE2E5847 CRC64;
     MIKRDLYYER IPTKSLREDV RYLGDVLGRV IKKQEGQSFF KLVEDTRLLS KANLANKHVK
     DPFKNILNKI KNLNPENTFK LARAFNHFMN FINLSETTDA SRKLDEYENN KKNSNKNIFI
     EEIFEKLFKD KKITNKKIYD VAKKLNIGIV LTAHPTEVKR RTLIQKYNKI IKILEQRDLY
     KKNLSKLKTL DKDLYNEITI IWNTDELKRS KPTPSEEARW GLAVIEDSLW DSIPKVYRRL
     NNIFLKNMGK SLPRNFNPIE FGSWMGGDRD GNPNVTAKVT SEALLLSRWE AAKLYEKQLT
     NLIRSLSMKK CSTQILNITG KTFEPYRVFL RPLRDKLRAT HILIKEHLVN KEPLDHKKLL
     SNTGEILTPL RVVRDSLIQN QSENIAEGDL LDLIRRARCF GINLAKLDIR QESSRHTKLI
     SEIVKKKYNK DYFLWNESEK LAFLSSRIKS KKNLIKNSLL KNKENKEVWS TFNVLVDQPK
     ECLGAYVISM TSAASDILSV AYLQKEAKIV NKLRVVPLFE TLDDLRNAKS IMNSLFSLPW
     YRKSINYKQE IMIGYSDSSK DAGKLSASWH QYKLQDEILK LAKKYKIDIT FFHGRGGSAG
     RGGGPIQATL KSQPANSVNG KIRITDQGEV IQQKYGYEPL AKYNLCSYIG AVVQATLNPP
     PEPKIKWKQL IEKMSEISMK SYRSNINEKS DFIRYFRTVT PHKALGKLSI GSRPSKRKNV
     DNIQSLRAIP WVFAWTQIRL FLPAWLGTTE ALNYASSKVF KKILVDMEKN WPFFNSTMDI
     LDMVISKVDP EISKVYENQL ADKKLKIVGK KLRSQFETLK RLNKVITPFQ IRKQRKVFRT
     SVIIRNIYSE VLHITQSIVM KKLTLKKLNK NKKQHLADAL MTSIAGISAA MKNTG
//