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Database: UniProt/TrEMBL
Entry: A0A0H3MY84_STRS4
LinkDB: A0A0H3MY84_STRS4
Original site: A0A0H3MY84_STRS4 
ID   A0A0H3MY84_STRS4        Unreviewed;       898 AA.
AC   A0A0H3MY84;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 13.
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   ECO:0000313|EMBL:CAZ55369.1};
GN   OrderedLocusNames=SSUBM407_0535 {ECO:0000313|EMBL:CAZ55369.1};
OS   Streptococcus suis (strain BM407).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=568814 {ECO:0000313|EMBL:CAZ55369.1, ECO:0000313|Proteomes:UP000009077};
RN   [1] {ECO:0000313|EMBL:CAZ55369.1, ECO:0000313|Proteomes:UP000009077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BM407 {ECO:0000313|EMBL:CAZ55369.1,
RC   ECO:0000313|Proteomes:UP000009077};
RX   PubMed=19603075; DOI=10.1371/journal.pone.0006072;
RA   Holden M.T.G., Hauser H., Sanders M., Ngo T.H., Cherevach I.,
RA   Cronin A., Goodhead I., Mungall K., Quail M.A., Price C.,
RA   Rabbinowitsch E., Sharp S., Croucher N.J., Chieu T.B., Mai N.T.H.,
RA   Diep T.S., Chinh N.T., Kehoe M., Leigh J.A., Ward P.N., Dowson C.G.,
RA   Whatmore A.M., Chanter N., Iversen P., Gottschalk M., Slater J.D.,
RA   Smith H.E., Spratt B.G., Xu J., Ye C., Bentley S., Barrell B.G.,
RA   Schultsz C., Maskell D.J., Parkhill J.;
RT   "Rapid evolution of virulence and drug resistance in the emerging
RT   zoonotic pathogen Streptococcus suis.";
RL   PLoS ONE 4:E6072-E6072(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: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; FM252032; CAZ55369.1; -; Genomic_DNA.
DR   RefSeq; WP_012775556.1; NC_012926.1.
DR   RefSeq; YP_003028298.1; NC_012926.1.
DR   EnsemblBacteria; CAZ55369; CAZ55369; SSUBM407_0535.
DR   GeneID; 8153162; -.
DR   KEGG; ssb:SSUBM407_0535; -.
DR   PATRIC; fig|568814.3.peg.562; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000009077; 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   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
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:UP000009077};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:CAZ55369.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:CAZ55369.1}.
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;  102926 MW;  5B66BFF441C36950 CRC64;
     MAIQKLENYN NKEAIREEVT ILTSILEEVA AQMMPAETFA KIVELSQLSR QDDYQALIAI
     ISQLNNDELA VISRYFAVLP LLINISEDVD LAYEINHQNN IDQDYLGKIS TTIDMVSKQE
     NAAEILEKLN VVPVLTAHPT QVQRQSMLDL TKHIHELLRR YRDVKLGLLN KNKWEDELRY
     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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