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Database: UniProt/TrEMBL
Entry: H8NV27_RAHAQ
LinkDB: H8NV27_RAHAQ
Original site: H8NV27_RAHAQ 
ID   H8NV27_RAHAQ            Unreviewed;       881 AA.
AC   H8NV27;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   28-MAR-2018, entry version 40.
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=Q7S_21855 {ECO:0000313|EMBL:AFE60576.1};
OS   Rahnella aquatilis HX2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Rahnella.
OX   NCBI_TaxID=1151116 {ECO:0000313|EMBL:AFE60576.1, ECO:0000313|Proteomes:UP000007594};
RN   [1] {ECO:0000313|EMBL:AFE60576.1, ECO:0000313|Proteomes:UP000007594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HX2 {ECO:0000313|EMBL:AFE60576.1};
RX   PubMed=23144397; DOI=10.1128/JB.01769-12;
RA   Guo Y., Jiao Z., Li L., Wu D., Crowley D.E., Wang Y., Wu W.;
RT   "Draft Genome Sequence of Rahnella aquatilis Strain HX2, a Plant
RT   Growth-Promoting Rhizobacterium Isolated from Vineyard Soil in
RT   Beijing, China.";
RL   J. Bacteriol. 194:6646-6647(2012).
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; CP003403; AFE60576.1; -; Genomic_DNA.
DR   RefSeq; WP_013577573.1; NC_017047.1.
DR   EnsemblBacteria; AFE60576; AFE60576; Q7S_21855.
DR   GeneID; 34350171; -.
DR   KEGG; raa:Q7S_21855; -.
DR   PATRIC; fig|1151116.3.peg.4380; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000007594; 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};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007594};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:AFE60576.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AFE60576.1}.
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;  98793 MW;  ECA72AE2CB66F53A 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 PRHWEPSANT KEVLDTCQVI AEAPEGSIAA YVISMARTPS
     DVLAVHLLLK EAGCPFPMPV APLFETLDDL NNADDVMKQL LSIDWYRGFI QGKQMVMIGY
     SDSAKDAGVM AASWAQYRAQ DALIKTCEKA GIALTLFHGR GGSIGRGGAP AQAALLSQPP
     GSLKGGLRVT EQGEMIRFKF GLPEVTISSL ALYTSAILEA NLLPPPEPKQ AWVDIMEQLS
     DVSCKMYRGY VRENKDFVPY FRAATPEQEL AKLPLGSRPA KRKASGGVES LRAIPWIFAW
     TQNRLMLPAW LGAGAGLQAV VDDGKRDELE TMCRDWPFFS TRIGMLEMVF AKADLWLAEY
     YDHRLVGKEL WPLGQQLRDQ LASDIKVILA ISNDDHLMED LPWIAESIAL RNVYTDPLNV
     LQAELLHRSR ELEKDGKQDA NVEQALMVTI AGVAAGMRNT G
//
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