CAPP_STRA5
ID CAPP_STRA5 Reviewed; 931 AA.
AC Q8E0H2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=SAG0759;
OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=208435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-611 / 2603 V/R;
RX PubMed=12200547; DOI=10.1073/pnas.182380799;
RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT "Complete genome sequence and comparative genomic analysis of an emerging
RT human pathogen, serotype V Streptococcus agalactiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(2002).
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; AE009948; AAM99646.1; -; Genomic_DNA.
DR RefSeq; NP_687774.1; NC_004116.1.
DR RefSeq; WP_000019267.1; NC_004116.1.
DR AlphaFoldDB; Q8E0H2; -.
DR SMR; Q8E0H2; -.
DR STRING; 208435.SAG0759; -.
DR EnsemblBacteria; AAM99646; AAM99646; SAG0759.
DR KEGG; sag:SAG0759; -.
DR PATRIC; fig|208435.3.peg.765; -.
DR HOGENOM; CLU_006557_2_0_9; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000000821; 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; Reference proteome.
FT CHAIN 1..931
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166626"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT ACT_SITE 594
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ SEQUENCE 931 AA; 105962 MW; F5338365FADF9B2C CRC64;
MSHPKLESSS NKEIITEEVG LLKQLLDEAT QKLIGSESFD KIEKIVSLSL TDDYTGLKET
ISALSNEEMV IVSRYFSILP LLINISEDVD LAYEINYKNN LNQDYLGKLS TTIDVVAGHE
NAKDILEHVN VVPVLTAHPT QVQRKTVLEL TSKIHDLLRK YRDVKAGIVN QEKWYADLRR
YIGIIMQTDT IREKKLKVKN EITNVMEYYN RSLIKAVTKL TAEYKALAAK KGIHLENPKP
LTMGMWIGGD RDGNPFVTAE TLRLSAMVQS EVIINHYIEQ LNELYRNMSL SINLTEVSPE
LVTLANQSQD NSVYRENEPY RKAFNFIQDK LVQTLLNLKV GSSPKEKFVS RQESSDIVGR
YIKSHIAQVA SDIQTEELPA YATAEEFKQD LLLVKQSLVQ YGQDSLVDGE LACLIQAVDI
FGFYLATIDM RQDSSINEAC VAELLKSANI VDDYSSLSEE EKCQLLLKEL TEDPRTLSST
HAPKSELLQK ELAIFQTARE LKDQLGEDII NQHIISHTES VSDMFELAIM LKEVGLIDAN
QARIQIVPLF ETIEDLDNSR DIMTQYLHYE LVKKWIATNN NYQEIMLGYS DSNKDGGYLS
SGWTLYKAQN ELTKIGEENG IKITFFHGRG GTVGRGGGPS YEAITSQPFG SIKDRIRLTE
QGEIIENKYG NQDAAYYNLE MLISASIDRM VTRMITNPNE IDNFRETMDG IVSESNAVYR
NLVFDNPYFY DYFFEASPIK EVSSLNIGSR PAARKTITEI SGLRAIPWVF SWSQNRIMFP
GWYGVGSAFK HFIEQDEANL AKLQTMYQKW PFFNSLLSNV DMVLSKSNMN IALQYAQLAG
SKEVRDVFNI ILNEWQLTKD MILAIEQHDN LLEENPMLHA SLDYRLPYFN VLNYVQIELI
KRLRSNQLDE DYEKLIHITI NGIATGLRNS G