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Database: UniProt/TrEMBL
Entry: W0L8H8_9GAMM
LinkDB: W0L8H8_9GAMM
Original site: W0L8H8_9GAMM 
ID   W0L8H8_9GAMM            Unreviewed;       878 AA.
AC   W0L8H8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   22-NOV-2017, entry version 33.
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   ORFNames=Z042_11185 {ECO:0000313|EMBL:AHG20123.1};
OS   Chania multitudinisentens RB-25.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Chania.
OX   NCBI_TaxID=1441930 {ECO:0000313|EMBL:AHG20123.1, ECO:0000313|Proteomes:UP000019030};
RN   [1] {ECO:0000313|EMBL:AHG20123.1, ECO:0000313|Proteomes:UP000019030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB-25 {ECO:0000313|EMBL:AHG20123.1,
RC   ECO:0000313|Proteomes:UP000019030};
RA   Robson E.H.J.;
RT   "Isolation of Serratia multitudinisentens RB-25 from Ex-Landfill
RT   site.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AHG20123.1, ECO:0000313|Proteomes:UP000019030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB-25 {ECO:0000313|EMBL:AHG20123.1,
RC   ECO:0000313|Proteomes:UP000019030};
RA   Chan K.-G.;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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; CP007044; AHG20123.1; -; Genomic_DNA.
DR   RefSeq; WP_024913967.1; NZ_JAJC01000034.1.
DR   EnsemblBacteria; AHG20123; AHG20123; Z042_11185.
DR   GeneID; 32578010; -.
DR   KEGG; sfo:Z042_11185; -.
DR   PATRIC; fig|1441930.4.peg.2224; -.
DR   KO; K01595; -.
DR   Proteomes; UP000019030; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019030};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:AHG20123.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AHG20123.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019030}.
FT   COILED      104    131       {ECO:0000256|SAM:Coils}.
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   878 AA;  98714 MW;  0992C4D0F3100072 CRC64;
     MNEQYSAMRS NVSMLGKLLG DTIKEALGEH ILDRVETIRK LSKSSRAGNE AHRQELLSTL
     QNLSNDELLP VARAFSQFLN LTNVAEQYHS ISPNGEAASN PEALAQLFTR LKDQKLNNKE
     LQNAVDELSI ELVLTAHPTE ITRRTLIHKL VEVNTCLSQL DHNDLADYER NKIMRRLRQL
     VAQSWHTDEI RKYRPSPVDE AKWGFAVVEN SLWEGVPAFL REFNEQLENS IDYRLPVEAV
     PVRFTSWMGG DRDGNPNVTA EITRHVLLLS RWKACDLFTR DIQVLVSELS MSECTPELRE
     LAGGDSVQEP YRELMKRLRS QLMSTQAYLE GRLKGERVLR PQDLLVNNEQ LWEPLYACYQ
     SLITCGMGII ANGQLLDTLR RVRCFGVPLV RIDVRQESTR HTEAIAELTR YLGLGDYESW
     SEADKQAFLI RELNSKRPLV PLNWKPSDET QEVLETCRVI AEAPQGSIAA YVISMARTPS
     DVLAVHLLLK EAGCPFALPV APLFETLDDL NNADDVMTQL LNIDWYRGFI QGKQMVMIGY
     SDSAKDAGVM AASWAQYRAQ DALIKTCEKA GVALTLFHGR GGSIGRGGAP AHAALLSQPP
     GSLKGGLRVT EQGEMIRFKF GLPEVTISSL ALYAGAVLEA NLLPPPEPKK EWRSLMDELS
     ETSCKMYRGY VRENPDFVPY FRAATPEQEL GKLPLGSRPA KRRPNGGVES LRAIPWIFAW
     TQNRLMLPAW LGAGAGLQEA VKAGKQEQLG AMCRDWPFFS TRIAMLEMVF SKTDLWLAEY
     YDQRLVDKSL WPLGKQLRDQ LESDIKVVLA IANDDNLMED LPWIAESIAL RNVYTDPLNV
     LQAELLHRSR QQEHPDARVE QALMVTIAGV AAGMRNTG
//
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