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Database: UniProt/TrEMBL
Entry: M9Y9N4_AZOVI
LinkDB: M9Y9N4_AZOVI
Original site: M9Y9N4_AZOVI 
ID   M9Y9N4_AZOVI            Unreviewed;       878 AA.
AC   M9Y9N4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   28-MAR-2018, entry version 37.
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   ECO:0000313|EMBL:AGK18546.1};
GN   ORFNames=AvCA6_39300 {ECO:0000313|EMBL:AGK18546.1};
OS   Azotobacter vinelandii CA6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=1283331 {ECO:0000313|EMBL:AGK18546.1, ECO:0000313|Proteomes:UP000012988};
RN   [1] {ECO:0000313|EMBL:AGK18546.1, ECO:0000313|Proteomes:UP000012988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CA6 {ECO:0000313|EMBL:AGK18546.1,
RC   ECO:0000313|Proteomes:UP000012988};
RA   Noar J.D., Bruno-Barcena J.M.;
RT   "Complete Genome Sequences of Azotobacter vinelandii Wild-Type Strain
RT   CA and Tungsten-Tolerant Mutant Strain CA6.";
RL   Genome Announc. 1:E00313-E00313(2013).
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; CP005095; AGK18546.1; -; Genomic_DNA.
DR   RefSeq; WP_012702445.1; NC_021150.1.
DR   ProteinModelPortal; M9Y9N4; -.
DR   EnsemblBacteria; AGK18546; AGK18546; AvCA6_39300.
DR   KEGG; avd:AvCA6_39300; -.
DR   PATRIC; fig|1283331.3.peg.3753; -.
DR   KO; K01595; -.
DR   Proteomes; UP000012988; 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:UP000012988};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AGK18546.1}.
FT   ACT_SITE    140    140       {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;  97414 MW;  CD91151FBD3AB608 CRC64;
     MEEIDARLRE DVRLLGELLG EYIHAQCGEV FFDKIERIRL GAKTGRLGSE EGAEQLTRTL
     GELREDELQP VARAFNQFLN LANIAEQYHE IRRRAPEEPP PFAVRALPEL LDRLLAGGHA
     ADALARQLGR LEIDLVLTAH PTEVTRRTLI RKYEAIAAEL AVLDHGDLLP AEREAVHERL
     RRLIAEAWHT DEIRRSRPTP VDEAKWGFSV IEHSLWQAVP AFLRGVDRAL HEATGLHLPL
     EAAPIRFSSW MGGDRDGNPN VTAAVTREVL LLARWAAADL HLRDVEQLAA ELSMQEASSE
     LRARTGEVDE PYRVLLKQLR ERLFATRDWA AAALHGEAVR SPAVLQNNRE LLQPLELCYR
     SLHACGMGLI ADGPLLDSLR RAATFGLFLV RLDIRQDAAR HAAALSEITE YLGLGRYADW
     NEETRTAFLM RELDSRRPLL PVHFPASAET AEVLATCREV AQAPAASLGS YVISMAAAPS
     DVLAVQLLLK ECGLQRPMRV VPLFETLTDL DNAAPTVERL LLLPGYRARL HGPQEVMIGY
     SDSAKDGGTT AAAWAQYRAQ EGLVEVCRRQ GVELLLFHGR GGTVGRGGGP AHAAILSQPP
     GSVPGRFRTT EQGEMIRFKF GLPDTAVQSL NLYLSAVLEA TLLPPPAPEP AWRELMDRLA
     AEGLAAYRSV VREHPQFVEY FRQATPEQEL GRLPLGSRPA KRRAGGIESL RAIPWIFAWT
     QTRLMLPAWL GWETALGNAL ARGEGELLRR MSRHWPFFGT RIDMLEMVLA KSDAAIAQLY
     DERLVEPGLL PLGQQLRGLL SQACAAVLEL TEQDRLLGHN PEVRAAFSVR NTYLDPLHLL
     QVELLARYRL HQEQACSPLE QALLVSVAGI AAGLRNTG
//
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