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Database: UniProt/TrEMBL
Entry: G7SFD4_STRSU
LinkDB: G7SFD4_STRSU
Original site: G7SFD4_STRSU 
ID   G7SFD4_STRSU            Unreviewed;       898 AA.
AC   G7SFD4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   07-JUN-2017, entry version 37.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
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:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=SSUD12_0519 {ECO:0000313|EMBL:AER18842.1};
OS   Streptococcus suis D12.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1004952 {ECO:0000313|EMBL:AER18842.1, ECO:0000313|Proteomes:UP000008845};
RN   [1] {ECO:0000313|EMBL:AER18842.1, ECO:0000313|Proteomes:UP000008845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D12 {ECO:0000313|EMBL:AER18842.1};
RX   PubMed=22026465; DOI=10.1186/1471-2164-12-523;
RA   Zhang A., Yang M., Hu P., Wu J., Chen B., Hua Y., Yu J., Chen H.,
RA   Xiao J., Jin M.;
RT   "Comparative Genomic Analysis of Streptococcus suis reveals
RT   significant genomic diversity among different serotypes.";
RL   BMC Genomics 12:523-523(2011).
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:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
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:SAAS00635168}.
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DR   EMBL; CP002644; AER18842.1; -; Genomic_DNA.
DR   RefSeq; WP_014637614.1; NC_017621.1.
DR   EnsemblBacteria; AER18842; AER18842; SSUD12_0519.
DR   KEGG; ssk:SSUD12_0519; -.
DR   PATRIC; fig|1004952.3.peg.503; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000008845; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
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   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:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008845};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AER18842.1}.
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;  102862 MW;  9ABD6CC668726CF3 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
     IKQSLIENKS MALLKGDFTE LLEAVEAFGF YLASIDMRQD SSIHEASVAE LLASARIVED
     YSSLSEEAKC HVLLKQLETD PRILSATHIP 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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