ID Q1PK86_PROMR Unreviewed; 989 AA.
AC Q1PK86;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 28-JUN-2023, entry version 70.
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:ABE11140.1};
GN ORFNames=HF10-11H11_0023 {ECO:0000313|EMBL:ABE11140.1};
OS uncultured Prochlorococcus marinus clone HF10-11H11.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=379375 {ECO:0000313|EMBL:ABE11140.1};
RN [1] {ECO:0000313|EMBL:ABE11140.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16556843; DOI=10.1126/science.1122050;
RA Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
RA Delong E.F., Chisholm S.W.;
RT "Genomic islands and the ecology and evolution of Prochlorococcus.";
RL Science 311:1768-1770(2006).
RN [2] {ECO:0000313|EMBL:ABE11140.1}
RP NUCLEOTIDE SEQUENCE.
RG US DOE Joint Genome Institute (JGI);
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Richardson P.;
RT "Sequencing of the draft fosmids and assembly of Prochlorococcus marinus
RT environmental genome fragment.";
RL Submitted (APR-2006) 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; DQ366723; ABE11140.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1PK86; -.
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:ABE11140.1}.
FT ACT_SITE 175
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 630
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 989 AA; 114176 MW; 50FB16A63B7DF59F CRC64;
MESFRQIKNN NVDLISNNDP LDKNRLLIED LWESVLREEC PDDQAERLIQ LKELSYSKQI
DGDSSKTFKN EIVDIVNSMD LAESIAAARA FSLYFQLVNI LEQRVEEDRY IQSFTNKDVQ
KSPDNLDPFA PALARQNAPV TFRELFYRLR KLNVPPGKLE ELLQEMDIRL VFTAHPTEIV
RHTIRHKQTR VANLLKKIQI EQFLTKEEKI SLKTQLKEEV RLWWRTDELH QFKPSVLDEV
DYALHYFQQV LFNAMPQLRG RVAEALTENY PDVQLPPESF CNFGSWVGSD RDGNPSVTPE
ITWRTACYQR QLMLERYVIA TSNLRDQLSV SMQWSQVSSS LLESLETDRV KFPEIYEARA
TRYRSEPYRL KLSYILEKLR LTQERNNLLA DSGWKFDLEG EIDNKNIDKV ENLYYKSINE
FTYDLELIKN SLISTDLTCE SVNNLLTQVH IFGFSLASLD IRQESTRHSD AIQELTNYLD
LSVQYDQMSE EEKIKWLIDE LNTKRPLIPS DVNWTKTTEE TFSVFKMVKR LQQEFGSRIC
HSYVISMSHS ASDLLEVLLL AKEMGLLDQN SQKSKLLVVP LFETVEDLKR APAVMEQLFK
LDFYKSLLPK VGESFKPLQE LMLGYSDSNK DSGFVSSNWE IHRAQIALQN LSSRNDILLR
LFHGRGGSVG RGGGPAYQAI LAQPSGTLKG RIKITEQGEV LASKYSLPEL ALYNLETVTT
AVIQNSLVNN RLDATPEWNQ LMSRLAETSR SHYRKLVHEN PDLLNFFQEV TPIEEISKLQ
ISSRPARRKK GAKDLSSLRA IPWVFGWTQS RFLLPSWFGV GTALSSELNS DPQQIELLRV
LHQRWPFFRM LISKVEMTLS KVDLEVARYY VDTLGSKENK DSFDNIFEVI SKEYNLTKSL
ILEITGKNKL LESDRDLKSS VSLRNKTIIP LGFLQVSLLR RLRDQTRQPP ISEFIIDKDE
SRRAYSRSEL LRGALLTING IAAGMRNTG
//
