CAPP_STRA3
ID CAPP_STRA3 Reviewed; 931 AA.
AC Q8E647;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
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=gbs0780;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(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}.
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; AL766847; CAD46424.1; -; Genomic_DNA.
DR RefSeq; WP_000019267.1; NC_004368.1.
DR AlphaFoldDB; Q8E647; -.
DR SMR; Q8E647; -.
DR STRING; 211110.gbs0780; -.
DR EnsemblBacteria; CAD46424; CAD46424; CAD46424.
DR KEGG; san:gbs0780; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_9; -.
DR OMA; PWVFGWT; -.
DR Proteomes; UP000000823; 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..931
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166625"
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