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Database: UniProt/TrEMBL
Entry: D5AGL8_STRGZ
LinkDB: D5AGL8_STRGZ
Original site: D5AGL8_STRGZ 
ID   D5AGL8_STRGZ            Unreviewed;       898 AA.
AC   D5AGL8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   22-NOV-2017, entry version 51.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=SSGZ1_0518 {ECO:0000313|EMBL:ADE30983.1};
OS   Streptococcus suis (strain GZ1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=423211 {ECO:0000313|EMBL:ADE30983.1, ECO:0000313|Proteomes:UP000002359};
RN   [1] {ECO:0000313|EMBL:ADE30983.1, ECO:0000313|Proteomes:UP000002359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GZ1 {ECO:0000313|EMBL:ADE30983.1,
RC   ECO:0000313|Proteomes:UP000002359};
RX   PubMed=19016627; DOI=10.1086/594370;
RA   Ye C., Zheng H., Zhang J., Jing H., Wang L., Xiong Y., Wang W.,
RA   Zhou Z., Sun Q., Luo X., Du H., Gottschalk M., Xu J.;
RT   "Clinical, experimental, and genomic differences between
RT   intermediately pathogenic, highly pathogenic, and epidemic
RT   Streptococcus suis.";
RL   J. Infect. Dis. 199:97-107(2009).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP000837; ADE30983.1; -; Genomic_DNA.
DR   RefSeq; WP_011922076.1; NC_017617.1.
DR   SMR; D5AGL8; -.
DR   EnsemblBacteria; ADE30983; ADE30983; SSGZ1_0518.
DR   KEGG; ssw:SSGZ1_0518; -.
DR   PATRIC; fig|423211.3.peg.508; -.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000002359; 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 {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002359};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ADE30983.1}.
FT   ACT_SITE    138    138       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    561    561       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   898 AA;  102866 MW;  678102D294644EFD CRC64;
     MAIQKLENYN NKEAIREEVT ILTSILEEVA AQMMPAETFA KIVELSQLSR QDDYQALIAI
     ISQLNNDELA VISRYFAVLP LLINISEDVD LAYEINHQNN IDQDYLGKIS TTIDMVSKQE
     NAAEILEKLN VVPVLTAHPT QVQRQSMLDL TKHIHELLRR YRDVKLGLLN KNKWEDELRC
     YIEIIMQTDM IREKKLKVTN EITNVMEYYN SSFIKAVTKL QREYKRLAAE KGIVLNNPRP
     ITMGMWIGGD RDGNPFVTAE TLKLSALTQC EVIMNYYDEQ LYKLYRNFSL STSIVNVSTA
     VKMLADLSED SSVYRENEPY RRAFHYIQMK LANTRDYLVH NKPSDVRYSN VAEFKADLLA
     IKQSLVENKS MALLKGDFTE LLEAVEAFGF YLASIDMRQD SSIHEASVAE LLASARIVED
     YSSLSEEAKC HVLLKQLETD PRILSATHMP KSEQLEKELA IFAAARELKD KLGEEIIKQH
     IISHSESVSD LLELAVLLKE VGLVDVDKAR VQIVPLFETI EDLDNAPDTM RQYLQLDLAK
     RWIAGNKYYQ EIMLGYSDSN KDGGYLSSGW TLYKAQNELT QIGQDYGVNI TFFHGRGGTV
     GRGGGPSYDA ITSQPFGSIK DRLRLTEQGE VIGNKYGNKD AAYYNLEMLV SATLDRMVTQ
     MITDPNEIDG YRETMDEIVS DSYRIYRDLV FNNPHFYDYF FAASPIREVS SLNIGSRPAA
     RKTITEIGGL RAIPWVFSWS QNRVMLPGWY GVGSSFKRFI DKHPDNLSKL QKMYESWPFF
     RSLLSNVDMV LSKSNMNIAF EYAKMCESEE VRNIFHVILD EWQLTKEIIL SIEQNDELLA
     ELPFLKASLD YRMPYFNVLN YIQIELIHRL RRGELSKEQE NLIHITINGV ATGLRNSG
//
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