ID Q46IP1_PROMT Unreviewed; 994 AA.
AC Q46IP1;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 105.
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=PMN2A_1147 {ECO:0000313|EMBL:AAZ58637.1};
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ58637.1, ECO:0000313|Proteomes:UP000002535};
RN [1] {ECO:0000313|EMBL:AAZ58637.1, ECO:0000313|Proteomes:UP000002535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A {ECO:0000313|EMBL:AAZ58637.1,
RC ECO:0000313|Proteomes:UP000002535};
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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; CP000095; AAZ58637.1; -; Genomic_DNA.
DR RefSeq; WP_011295491.1; NC_007335.2.
DR AlphaFoldDB; Q46IP1; -.
DR STRING; 59920.PMN2A_1147; -.
DR KEGG; pmn:PMN2A_1147; -.
DR HOGENOM; CLU_006557_2_0_3; -.
DR OrthoDB; 9768133at2; -.
DR PhylomeDB; Q46IP1; -.
DR Proteomes; UP000002535; 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:AAZ58637.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002535}.
FT ACT_SITE 178
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 634
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 994 AA; 113292 MW; 30DFA0C823B3A0CE CRC64;
MLKNPSNENI SNHSTVCVED QDPGSLLQQR LELVEDLWKT VLKSECPPDQ TERLLRLKQL
SDPSKSNQDN SSKAIVQLIT KMDLAEAISA ARAFSLYFQL VNILEQRIEE DSYLESIEKG
KLDTSNYKID PFAPALASQT APATFTQLFE RLRRLNVPPA QLDGLMREMD IRLVFTAHPT
EIVRHTVRHK QRRVATLLQQ LQSNSLISES EKEIFRLQLE EEIRLWWRTD ELHQFKPTVL
DEVDYALHYF QQVLFDAMPQ LRRRLTTALA SSYPDVEIPN EAFCTFGSWV GSDRDGNPSV
TPEITWRTAC YQRQLMLDRY IASVQDLRDQ LSISMQWSQV SSPLLESLEM DRVRFPEVYE
ERAARYRLEP YRLKLSYTLE RLRLTQLRNK QLADAGWQFS PDGKPLISTN NSFDEVLHYK
SVEELKNELE LIRNSLVSTD LTCEPLDTLL NQVHIFGFSL ASLDIRQEST RHSDALDELT
RYLDLPESYG VMSEESRVQW LMKELRTRRP LIPPSFEWSK STQETISVFH MLHRLQKEFG
TRICRSYVIS MSHTASDLLE VLLLAKESGL IDPTLGASDL LVVPLFETVE DLQHAPSVME
SLLQTDVYRE LLPRVGEKKQ PLQELMLGYS DSNKDSGFLS SNWEIHKAQI ALQDLASRQG
IALRIFHGRG GSVGRGGGPA YQAILAQPSG TLQGRIKITE QGEVLASKYS LPELALYNLE
TVTTAVIQNS LVTNKLDATP SWNELMTRLA ARSREHYRAL VHDNPDLVQF FQVVTPIEEI
SKLQISSRPA RRKSGAKDLS SLRAIPWVFG WTQSRFLLPS WFGVGTALAT ELKADPDQME
MLRMLNQRWP FFRMLISKVE MTLSKVDLDV AHHYVVSLGG SDDRDAFARI FDIISSEYSL
TKKLILEITG KSKLLSADPA LQLSVNLRNR TIVPLGFLQV ALLKRLRDQN RQPPISEDVS
IDSTQSSRTY SRSELLRGAL LTINGIAAGM RNTG
//
