(data stored in SCRATCH zone)

SWISSPROT: D3VH32_XENNA

ID   D3VH32_XENNA            Unreviewed;       879 AA.
AC   D3VH32;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 61.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS01082397};
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:SAAS01082397};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:CBJ88317.1};
GN   OrderedLocusNames=XNC1_0229 {ECO:0000313|EMBL:CBJ88317.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88317.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88317.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(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:SAAS01082398}.
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;
CC         EC=4.1.1.31; Evidence={ECO:0000256|HAMAP-Rule:MF_00595,
CC         ECO:0000256|SAAS:SAAS01118615};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS01082409};
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:SAAS01082401}.
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DR   EMBL; FN667742; CBJ88317.1; -; Genomic_DNA.
DR   STRING; 406817.XNC1_0229; -.
DR   EnsemblBacteria; CBJ88317; CBJ88317; XNC1_0229.
DR   KEGG; xne:XNC1_0229; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000008075; 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;
DR   PRODOM; D3VH32.
DR   SWISS-2DPAGE; D3VH32.
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS01082400};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS01082405,
KW   ECO:0000313|EMBL:CBJ88317.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS01082403};
KW   Pyruvate {ECO:0000313|EMBL:CBJ88317.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   ACT_SITE    137    137       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    545    545       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   879 AA;  98605 MW;  81E50940A6F8C677 CRC64;
     MNQQYSAMRS NVSMLGKLLG DTIKEALGED ILDKVETIRK LSKSSRAGNE VHRQQLLSTL
     ENLSNDELLP VARAFNQFLN LANAAEQYHS ISPHGEAASN PVALAALFNR LKDKQFSNDD
     LVKAIDELAI ELVLTAHPTE IARRTLIHKL VEVNGCLAQL DHDDLADYER NNIMRRLRQL
     IAQSWHTDEI RKIRPTPIDE AKWGFAVVEN SLWEGVPAFL REFNEQLEES IGYSLPVEAV
     PVRFTSWMGG DRDGNPNVTA DITRHVLLLS RWKAADLFLK DIQILVSELS MSECTPEVRQ
     MAGGDHVLEP YREIAKQLRT QLSHTLAYLE KCLKGEQVLP PSDLLLHNEQ LWQPLYACYQ
     SLKACGMEII ANGQLLDTLR RIRCFGLCLV RIDIRQESTR HTDAIAELTQ YLEMGDYASW
     PEAEKQAFLL HELNSKRPLT PRDWQPSAET QEVFETCKVI AETPQDAIAA YVISMAKVPS
     DVLAVKLLLK EAGCSLSLPV APLFETLDDL NNAESVIRKL LGITWYRELI QDKQMVMIGY
     SDSAKDAGVM AASWAQYQAQ DALIKVCEQE GVTLTLFHGR GGTIGRGGAP AHSALLSQPP
     GSLKGGLRVT EQGEMIRFKF GLPQVAISSL ALYASAILEA NLLPPPEPKP EWRQIMGILS
     DVSCNMYRDY VREQPEFVPY FRAATPEQEL AKLPLGSRPA KRRPTGGVES LRAIPWIFAW
     TQNRLMLPTW LGAGAALQQV IDAGKLSVLT DMSRDWPFFN TRIAMLEMVF AKADLWLAEY
     YDQRLVDPKL WPLGLKLRNQ LAEDIKTVLT ISQDEQLMAD LPWIAESIAL RNVYTDPLNV
     LQVELLQRSR QQEEALDPHL EQALMVTIAG VAAGMRNTG
//

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