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Database: UniProt/TrEMBL
Entry: B1WNZ1_CYAA5
LinkDB: B1WNZ1_CYAA5
Original site: B1WNZ1_CYAA5 
ID   B1WNZ1_CYAA5            Unreviewed;      1020 AA.
AC   B1WNZ1;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 73.
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   ECO:0000313|EMBL:ACB53170.1};
GN   OrderedLocusNames=cce_3822 {ECO:0000313|EMBL:ACB53170.1};
OS   Cyanothece sp. (strain ATCC 51142).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece.
OX   NCBI_TaxID=43989 {ECO:0000313|EMBL:ACB53170.1, ECO:0000313|Proteomes:UP000001203};
RN   [1] {ECO:0000313|EMBL:ACB53170.1, ECO:0000313|Proteomes:UP000001203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51142 {ECO:0000313|EMBL:ACB53170.1,
RC   ECO:0000313|Proteomes:UP000001203};
RX   PubMed=18812508; DOI=10.1073/pnas.0805418105;
RA   Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C.,
RA   Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R.,
RA   Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.;
RT   "The genome of Cyanothece 51142, a unicellular diazotrophic
RT   cyanobacterium important in the marine nitrogen cycle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595}.
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; CP000806; ACB53170.1; -; Genomic_DNA.
DR   ProteinModelPortal; B1WNZ1; -.
DR   STRING; 43989.cce_3822; -.
DR   EnsemblBacteria; ACB53170; ACB53170; cce_3822.
DR   KEGG; cyt:cce_3822; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000001203; Chromosome circular.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-HAMAP.
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; 2.
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:UP000001203};
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:ACB53170.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001203}.
FT   ACT_SITE    197    197       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    667    667       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1020 AA;  117283 MW;  3BAACD5E8385A87C CRC64;
     MLLVMLLESL QSTVEEVNIF STSDLFLRQR LKLVESLWES VLKAECGQEL VDLLEKLRKI
     CSPEGQVTDK PKTSINELIE GLELNEAIRA ARAFALYFQL INIVEQHYEQ RDQQLNRRAT
     YQESEKARNN HAKEENKANG SVGADLLEKA LVGGTENQEK GGTFHWLFPQ LKRLNVPPQQ
     IQRLLEQLDI RLVFTAHPTE IVRHTIRLKQ RRIATLLRRL DYAEESFRGM GLSSSWEAES
     IIEQLNEEIR LWWRTDELHQ FKPSVLDEVD YTLHYFDEVL CDALPQLSQR LQQALKANFP
     RIKPPHNTFC RFGSWVGGDR DGNPFVTPEV TWRTACYQRN LILEKYLAAI EDLTEILSSS
     LHWSNVSQDL LDSLERDRVA MPEIYDELAI RYRQEPYRLK LAYIEKRLET TRDRNNHLAN
     PEKRQILTEE TPPNIYHSGE EFEAELQLIK RNLEETGLKC QALENLIFQA QMFGFTLTQL
     DFRQESSRHS ETIEVIANYL NVLPRPYGEL SETEKVNWLV GELQTRRPLI PMEMPFDEKT
     IETIETMRML RYLQQEFGVE ICQTYIISMT NDVSDVLEVL LLAKEAGLYD PGTSTTTIRI
     VPLFETVDDL KRAPEIMDAL FKLTLYRAAL AGGYDYLDEA KKEQLPPPEL QPANLQEIMV
     GYSDSNKDSG FLSSNWEIHK AQKSLQKVAE PYGLALRLFH GRGGSVGRGG GPAYAAILAQ
     PTGTINGRIK ITEQGEVLAS KYSLPELALY NLETATTAVI QASLLGSGFD DIVPWNDIME
     ELASSARKAY RSLIYEQPDF LDFFLSVTPI PEISQLQISS RPARRKSGKK DLSTLRAIPW
     VFSWTQSRFL LPAWYGVGTA LESFLQQEPN ENLKLLRYFY LKWPFFKMVI SKVEMTLSKV
     DLQIAHHYVK ELSQPEDIER FNKVFERISQ EYHRTRDIIL SINEQPKLLE GDAGLQRSVQ
     LRNGTIVPLG FLQVSLLKRL RQYTRQAESG VIHFRYSKEE LLRGALLTIN GIAAGMRNTG
//
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