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Database: UniProt/TrEMBL
Entry: A0A0S2KB55_9GAMM
LinkDB: A0A0S2KB55_9GAMM
Original site: A0A0S2KB55_9GAMM 
ID   A0A0S2KB55_9GAMM        Unreviewed;       856 AA.
AC   A0A0S2KB55;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   20-DEC-2017, entry version 12.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   ORFNames=PS2015_856 {ECO:0000313|EMBL:ALO45528.1};
OS   Pseudohongiella spirulinae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudohongiella.
OX   NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO45528.1, ECO:0000313|Proteomes:UP000065641};
RN   [1] {ECO:0000313|EMBL:ALO45528.1, ECO:0000313|Proteomes:UP000065641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO45528.1,
RC   ECO:0000313|Proteomes:UP000065641};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC       {ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00946766};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP013189; ALO45528.1; -; Genomic_DNA.
DR   RefSeq; WP_058021059.1; NZ_CP013189.1.
DR   EnsemblBacteria; ALO45528; ALO45528; PS2015_856.
DR   KEGG; pspi:PS2015_856; -.
DR   PATRIC; fig|1249552.3.peg.861; -.
DR   KO; K01595; -.
DR   Proteomes; UP000065641; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PTHR30523; 2.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|SAAS:SAAS00946757};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000065641};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ALO45528.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000065641}.
FT   COILED      284    304       {ECO:0000256|SAM:Coils}.
FT   COILED      609    636       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   856 AA;  98090 MW;  817C5A00EF2E0390 CRC64;
     MSNETARLFE ELVALNYQLY SSLFLKLPLD AIEQTGTLLP LLSEACERGL SEGKNAKSII
     GEFFEQHREH FNEHEQIQFL FKIIQYVERQ VVLIDALEDA AYSRIHQIDN KTSLIRLTER
     AADDGRTDKL AQLLKNFGVR VVLTAHPTQF YPGQVLAIIS DLTEAISGAR TGEVRDLLQQ
     LGNTPFFQKQ KPSPYDEAVL LTWYLSNIFY QAIGELVDPL AQRFPEQINS NAELVSIGFW
     PGGDRDGNPF VTTDTTLRVA ARLRQSIIQC YHNDIRQLKR RLSFRDVYEA LDKLEKQLRD
     ELSEKPGREG VLLSDIHLVL DQVERLLSER YQSMYIDSLQ SFRRKVTLFG FHFASIDIRQ
     DSRVIARTLE SIVQQQPGLL PMDFNSLNED QQINAMLACK GEVDASRFDD PVIRDTIESF
     SVIRRIQFTN GERGAHRYII SNCRGPVDVV RVLTLFRLCG WRDRPINVDI VPLFETIDDL
     QRAGESMARL YANTQYQVHL SHRRQRQTVM LGFSDGTKDG GYLMANWGIY TAKEDVTAVS
     RDQGVEVIFF DGRGGPPARG GGDTYLFYAA HGRTIESNQI QMTVQGQTIS SYYGIKDAAK
     HNLGQLLTAG LENNLLDRVD RELDDLQRNL IRDLAERSYQ KYEAFKNHKL FMPYLEEMST
     LKYYAMANIG SRPSKRGGGD AMKFEDLRAI PFVGAWSQLK QNVPGFYGLG SALKAQEELG
     RLDACLELYE HSRFFRALIS NSMQSMSKTN FELTRYMEND PQFGEFWQDI YQEYLISKEM
     VLKISGQDQL LQDNPRSRMS IRLREEVVLP LLTIQQYALI RIRECREQDA AEQLAMYEKM
     VVRTLFGNIN AARNSA
//
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