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Database: UniProt/TrEMBL
Entry: Q3AWA1_SYNS9
LinkDB: Q3AWA1_SYNS9
Original site: Q3AWA1_SYNS9 
ID   Q3AWA1_SYNS9            Unreviewed;       995 AA.
AC   Q3AWA1;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   27-SEP-2017, entry version 85.
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=Syncc9902_1933 {ECO:0000313|EMBL:ABB26890.1};
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB26890.1, ECO:0000313|Proteomes:UP000002712};
RN   [1] {ECO:0000313|Proteomes:UP000002712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) 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}.
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; CP000097; ABB26890.1; -; Genomic_DNA.
DR   RefSeq; WP_011360692.1; NC_007513.1.
DR   ProteinModelPortal; Q3AWA1; -.
DR   STRING; 316279.Syncc9902_1933; -.
DR   EnsemblBacteria; ABB26890; ABB26890; Syncc9902_1933.
DR   KEGG; sye:Syncc9902_1933; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000002712; 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:UP000002712};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ABB26890.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ABB26890.1}.
FT   ACT_SITE    183    183       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    637    637       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   995 AA;  112790 MW;  FE1B0B342EBD8CDD CRC64;
     MPESTAHALQ GEQPRESGVT AGAGRLLQNR LVLVEDLWQT VLRSECPPEQ SARLLRLKQL
     SDPVALEGRD GDSTSEAIVE LIRAMDLSEA IAAARAFSLY FQLINILEQR IEEDSYLDSL
     APRKSAADDG RDAFDPFAPP LASQTDPATF GEVFERLRRM NVPPAQVEAL LQELDIRLVF
     TAHPTEIVRH TVRHKQRRVA NLLQQLQSDS PMALQVKDDL RQQLEEEIRL WWRTDELHQF
     KPTVLDEVDS TLHYFQQVLF DAMPQLRRRL TSSLHRHYPD VQVPQASFCT FGSWVGSDRD
     GNPSVTTDIT WRTACYQRQL MLELYISSVQ ALRNQLSISM QWSQVAPALL ESLEMDRLRF
     PEIYERRAAR YRLEPYRLKL SYILERLERT LKRNDQLSDA GWKSPKDAIP TDGPPGSEAL
     HYTSVDQFRN DLELIRNSLI GTELTCEQLD TLLHQVHIFG FSLASLDIRQ ESTRHSDAID
     ELTRFLELPQ PYGEMEESTR VAWLIEELRT RRPLIPTAVR WSDTTAETMA VFRMLHRLQE
     EFGQRICHSY VISMSHTASD LLEVLLLAKE AGLVDPAARK ASLLVVPLFE TVEDLQRAPA
     VMDELFNTPL YRDLLPMVGI QGQPLQELML GYSDSNKDSG FLSSNWEIHQ AQLALQELSS
     RQGVALRLFH GRGGSVSRGG GPAYQAILAQ PSGTLQGRIK ITEQGEVLAS KYSLPELALY
     NLETVTTAVV QNSLVTNQLD ATPSWNQLMS RLSARSREHY RALVHDNPDL VAFFQQVTPI
     EEISKLQISS RPARRKTGAK DLSSLRAIPW VFGWTQSRFL LPSWFGFGTA LAEEVKADPD
     QLDLLRRLHQ RWPFFRTLIS KVEMTLSKVD LDLAHHYMNS LGKPEQREAF EAIFAVIATE
     YALTRKLVLE ITGQPRLLGA DQGLQLSVDL RNRTIVPLGF LQVALLKRLR DQNRQPPMSE
     SPGAPEDTRT YSRSELLRGA LLTLNGIAAG MRNTG
//
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