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Database: UniProt/TrEMBL
Entry: H2IXG9_RAHAC
LinkDB: H2IXG9_RAHAC
Original site: H2IXG9_RAHAC 
ID   H2IXG9_RAHAC            Unreviewed;       881 AA.
AC   H2IXG9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-SEP-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   OrderedLocusNames=Rahaq2_4420 {ECO:0000313|EMBL:AEX54159.1};
OS   Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC
OS   105701 / NCIMB 13365 / CIP 78.65).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Rahnella.
OX   NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX54159.1, ECO:0000313|Proteomes:UP000009010};
RN   [1] {ECO:0000313|Proteomes:UP000009010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC   CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA   Martinez R., Woyke T.;
RT   "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL   Submitted (JAN-2012) 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: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; CP003244; AEX54159.1; -; Genomic_DNA.
DR   RefSeq; WP_015699176.1; NZ_JMPO01000146.1.
DR   STRING; 745277.Rahaq2_4420; -.
DR   EnsemblBacteria; AEX54159; AEX54159; Rahaq2_4420.
DR   KEGG; raq:Rahaq2_4420; -.
DR   PATRIC; fig|745277.3.peg.4228; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000009010; 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   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:UP000009010};
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:AEX54159.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009010}.
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   881 AA;  98822 MW;  CBAC1B03163CD22D CRC64;
     MNEQYSAMRS NVSTLGKLLG DTIKDTLGEH ILDRVEKIRK LSKSSRAGND ADRQELLSTL
     QNLSNDELLP VARAFSQFLN LANVAEQYHS ISPHGEAASN PEALAQLFDR LKSKNLSEQQ
     LRDAVDQLSI ELVLTAHPTE IARRTLIHKL VEVNNCLKQL DHNDLADYER KQIMRRLRQL
     IAQSWHTDEI RKNRPSPVDE AKWGFAVVEN SLWEGVPAFL RELNEQLETS LDYKMPVEAV
     PVRFTSWMGG DRDGNPNVTA DITRHVLLLS RWKATDLFLR DIAVLVSELS MTECTPELRE
     LAGGADIIEP YREIMKQLRS QLTNTQVYLE ARLKGERVAR PHDLLVKNDQ LWAPLYACYQ
     SLQACNMGII ANGQLLDTLR RVRCFGVPLV RIDVRQESTR HTDAIAEITR YLGLGDYESW
     SESDKQAFLI RELNSKRPLV PRHWEPSADT KEVLDTCQVI AEAPEGSIAA YVISMARTPS
     DVLAVHLLLK EAGCPFPMPV APLFETLDDL NNADDVMKQL LSIDWYRGFI QGKQMVMIGY
     SDSAKDAGVM AASWAQYRAQ DALIKTCEKA GIALTLFHGR GGSIGRGGAP AQAALLSQPP
     GSLKGGLRVT EQGEMIRFKF GLPEVTISSL ALYTSAILEA NLLPPPEPKQ AWVDIMEQLS
     DVSCKMYRGY IRENKDFVPY FRAATPEQEL AKLPLGSRPA KRKASGGVES LRAIPWIFAW
     TQNRLMLPAW LGAGAGLQAV VDGGKRDELE TMCRDWPFFS TRIGMLEMVF AKADLWLAEY
     YDHRLVEKEL WPLGQQLRDQ LASDIKVILA ISNDDHLMED LPWIAESIAL RNVYTDPLNV
     LQAELLHRSR ELEKDGKQDA NVEQALMVTI AGVAAGMRNT G
//
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