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CAPP_STRP2
ID   CAPP_STRP2              Reviewed;         898 AA.
AC   Q04KL8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=SPD_0953;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(2007).
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}.
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DR   EMBL; CP000410; ABJ54336.1; -; Genomic_DNA.
DR   RefSeq; WP_000058147.1; NC_008533.2.
DR   AlphaFoldDB; Q04KL8; -.
DR   SMR; Q04KL8; -.
DR   STRING; 373153.SPD_0953; -.
DR   PRIDE; Q04KL8; -.
DR   EnsemblBacteria; ABJ54336; ABJ54336; SPD_0953.
DR   GeneID; 60232607; -.
DR   KEGG; spd:SPD_0953; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_9; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   BioCyc; SPNE373153:G1G6V-1045-MON; -.
DR   Proteomes; UP000001452; 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..898
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025593"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        561
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   898 AA;  103209 MW;  DCDBCE2630E90ED0 CRC64;
     MSLQKLENSS NKSVVQEEVL ILTELLEDIT KNMLAPETFE KIIQLKELST QEDYQGLNRL
     VTSLSNDEMV YISRYFSILP LLINISEDVD LAYEINHQNN IDQDYLGKLS TTIKLVAEKE
     NAVEILEHLN VVPVLTAHPT QVQRKSMLDL TNHIHSLLRK YRDVKLGLIN KDKWYNDLRR
     YIEIIMQTDM IREKKLKVTN EITNAMEYYN SSFLKAVPHL TTEYKRLAQA HGLNLKQAKP
     ITMGMWIGGD RDGNPFVTAK TLKQSALTQC EVIMNYYDKK IYQLYREFSL STSIVNVSKQ
     VREMARQSKD NSIYREKELY RRALFDIQSK IQATKTYLIE DEEVGTRYET ANDFYKDLIA
     IRDSLLENKG ESLISGDFVE LLQAVEIFGF YLASIDMRQD SSVYEACVAE LLKSAGIHSR
     YSELSEEEKC DLLLKELEED PRILSATHAE KSELLAKELA IFKTARVLKD KLGDDVIRQT
     IISHATSLSD MLELAILLKE VGLVDTERAR VQIVPLFETI EDLDHSEETM RKYLSLSLAK
     KWIDSRNNYQ EIMLGYSDSN KDGGYLSSCW TLYKAQQQLT AIGDEFGVKV TFFHGRGGTV
     GRGGGPTYEA ITSQPLKSIK DRIRLTEQGE VIGNKYGNKD AAYYNLEMLV SAAINRMITQ
     KKSDTNTPNR YEAIMDQVVD RSYDIYRDLV FGNEHFYDYF FESSPIKAIS SFNIGSRPAA
     RKTITEIGGL RAIPWVFSWS QSRVMFPGWY GVGSSFKEFI NKNPENIAIL RDMYQNWPFF
     QSLLSNVDMV LSKSNMNIAF EYAKLCEDEQ VKAIYETILN EWQVTKNVIL AIEGHDELLA
     DNPYLKASLD YRMPYFNILN YIQLELIKRQ RRGELSSDQE RLIHITINGI ATGLRNSG
 
 
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