CAPP_PROM9
ID CAPP_PROM9 Reviewed; 989 AA.
AC Q318G7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=PMT9312_1667;
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=74546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_00595}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000111; ABB50728.1; -; Genomic_DNA.
DR RefSeq; WP_011377209.1; NC_007577.1.
DR AlphaFoldDB; Q318G7; -.
DR SMR; Q318G7; -.
DR STRING; 74546.PMT9312_1667; -.
DR EnsemblBacteria; ABB50728; ABB50728; PMT9312_1667.
DR KEGG; pmi:PMT9312_1667; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_3; -.
DR OMA; PWVFGWT; -.
DR OrthoDB; 398146at2; -.
DR Proteomes; UP000002715; 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 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; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation; Lyase; Magnesium.
FT CHAIN 1..989
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_1000025572"
FT ACT_SITE 175
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 630
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 989 AA; 114117 MW; D497EEFF87656186 CRC64;
MESFQQIKNN KVDLISTNDP LDKNRLLIED LWESVLREEC PDDQAERLIQ LKELSYSKQI
EGDSSKTFKK EIVDIVNSMD LAESIAAARA FSLYFQLVNI LEQRVEEDRY IQSFTNKNVQ
KSPDNLDPFA PALARQNAPV TFRELFYRLR KLNVPPGKLE ELLQEMDIRL VFTAHPTEIV
RHTIRHKQTR VANLLKKIQV EQFLTKEEKN FLKIQLKEEV RLWWRTDELH QFKPSVLDEV
DYALHYFQQV LFNAMPQLRG RIAEALTENY PDVQLPSQSF CNFGSWVGSD RDGNPSVTPE
ITWRTACYQR QLMLERYITA TSHLRDQLSV SMQWSQVSSS LLESLETDRV KFPAIYEARA
TRYRSEPYRL KLSYILEKLR LTQERNNLLA DNGWKFDLEG ELNTKNIDKV ENLYYKSVNE
FTYDLELIKN SLISTDLTCE AVNTLLTQVH IFGFSLASLD IRQESTRHSD AIQELTKYLD
LSVQYDQMSE DEKIKWLVDE LNTKRPLIPS DVKWTNTTEE TFSVFKMVKR LQQEFGSRIC
HAYVISMSHS ASDLLEVLLL AKEMGLLDQN SKNSNLLVVP LFETVEDLKR APEVMEKLFK
LDFYKSLLPK VGESFKPLQE LMLGYSDSNK DSGFVSSNWE IHRAQIALQN LASRNNILLR
LFHGRGGSVG RGGGPAYQAI LAQPSGTLKG RIKITEQGEV LASKYSLPEL ALYNLETVTT
AVIQNSLVNN RLDATPEWNQ LMSRLAETSR SHYRKLVYEN PDLLNFFQEV TPIEEISKLQ
ISSRPARRKK GAKDLSSLRA IPWVFGWTQS RFLLPSWFGV GTALSSELNS DPQQIELLRV
LHQRWPFFRM LISKVEMTLS KVDLEVAKYY VDTLGSEENK DSFDDIFEVI SKEYSLTKSL
VLEITGKNKL LESDRDLKSS VSLRNKTIIP LGFLQVSLLR RLRDQTRQPP ISEFLIDKDE
SRRAYSRSEL LRGALLTING IAAGMRNTG