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Database: UniProt/TrEMBL
Entry: A0A0E3JSM4_SULSF
LinkDB: A0A0E3JSM4_SULSF
Original site: A0A0E3JSM4_SULSF 
ID   A0A0E3JSM4_SULSF        Unreviewed;       511 AA.
AC   A0A0E3JSM4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-SEP-2017, entry version 14.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_01904};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_01904};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_01904};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_01904};
GN   Name=ppcA {ECO:0000256|HAMAP-Rule:MF_01904};
GN   ORFNames=SSOP1_2396 {ECO:0000313|EMBL:SAI85950.1}, SULA_0070
GN   {ECO:0000313|EMBL:AKA77915.1}, SULB_0071
GN   {ECO:0000313|EMBL:AKA72523.1}, SULC_0070
GN   {ECO:0000313|EMBL:AKA75222.1};
OS   Sulfolobus solfataricus.
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=2287 {ECO:0000313|EMBL:AKA72523.1, ECO:0000313|Proteomes:UP000033085};
RN   [1] {ECO:0000313|Proteomes:UP000033057, ECO:0000313|Proteomes:UP000033085, ECO:0000313|Proteomes:UP000033106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98/2 SULC {ECO:0000313|EMBL:AKA75222.1,
RC   ECO:0000313|Proteomes:UP000033057}, SULA {ECO:0000313|EMBL:AKA77915.1,
RC   ECO:0000313|Proteomes:UP000033106}, and SULB
RC   {ECO:0000313|EMBL:AKA72523.1, ECO:0000313|Proteomes:UP000033085};
RX   PubMed=26021927;
RA   McCarthy S., Gradnigo J., Johnson T., Payne S., Lipzen A., Martin J.,
RA   Schackwitz W., Moriyama E., Blum P.;
RT   "Complete Genome Sequence of Sulfolobus solfataricus Strain 98/2 and
RT   Evolved Derivatives.";
RL   Genome Announc. 3:e00549-15(2015).
RN   [2] {ECO:0000313|EMBL:SAI85950.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P1 {ECO:0000313|EMBL:SAI85950.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K.,
RA   Barbian K., Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the irreversible beta-carboxylation of
CC       phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-
CC       carbon dicarboxylic acid source for the tricarboxylic acid cycle.
CC       {ECO:0000256|HAMAP-Rule:MF_01904}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-
CC       Rule:MF_01904}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01904};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01904}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01904}.
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DR   EMBL; CP011055; AKA72523.1; -; Genomic_DNA.
DR   EMBL; CP011056; AKA75222.1; -; Genomic_DNA.
DR   EMBL; CP011057; AKA77915.1; -; Genomic_DNA.
DR   EMBL; LT549890; SAI85950.1; -; Genomic_DNA.
DR   RefSeq; WP_009991534.1; NZ_LT549890.1.
DR   EnsemblBacteria; AKA72523; AKA72523; SULB_0071.
DR   EnsemblBacteria; AKA75222; AKA75222; SULC_0070.
DR   EnsemblBacteria; AKA77915; AKA77915; SULA_0070.
DR   GeneID; 27428576; -.
DR   KEGG; ssoa:SULA_0070; -.
DR   KEGG; ssof:SULC_0070; -.
DR   KEGG; ssol:SULB_0071; -.
DR   PATRIC; fig|2287.6.peg.73; -.
DR   KO; K01595; -.
DR   Proteomes; UP000033057; Chromosome.
DR   Proteomes; UP000033085; Chromosome.
DR   Proteomes; UP000033106; Chromosome.
DR   Proteomes; UP000076770; Chromosome i.
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_01904; PEPcase_type2; 1.
DR   InterPro; IPR007566; PEP_COase_arc-type.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   Pfam; PF14010; PEPcase_2; 1.
DR   PIRSF; PIRSF006677; UCP006677; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR02751; PEPCase_arch; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033057,
KW   ECO:0000313|Proteomes:UP000033085, ECO:0000313|Proteomes:UP000033106,
KW   ECO:0000313|Proteomes:UP000076770};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Pyruvate {ECO:0000313|EMBL:AKA72523.1}.
SQ   SEQUENCE   511 AA;  58772 MW;  90E0795BB2EC2105 CRC64;
     MRIIPRTMST QHPDNAKVPE WAKSEVIEGE DEVKEAFLAY SMYGVHEVMW DAEGKDVDTH
     VVRKLLSNYP DYFREHILGK DLFLTYRLPN PKVEGADRKV FAETMESIPI TYDLAEKFYG
     NGITIPVFEV ILPMTTSSLE IISVARYYEK AVANEDELEL YDGVKVKDLV GEIYPKVIEV
     IPLVEDRDSL QNINNIVEGY YKVIKPKYMR VFLARSDPAM NYGMITAVLS VKIALSELYK
     LSESLNFEIY PIIGVGSLPF RGHLSPENYE KVLEEYKGVY TYTIQSAFKY DYDYDKVKSA
     ISSINNSRIS PARILEKYEE DVLRKITILY TERYQPIIES LANAINDVSV LLPRRRARKL
     HIGLFGYSRS AGKVSLPRAI SFVGSLYSIG IPPELIGISS LSNLDEKEWD IFKQNYVNFK
     HDLQTAARFL NWESFKLIKD IWKISEDTIA KIKEDIDYAE SVIGIKLGGI DYDSRKHILM
     SSLFLLSFKE KILQESKKYL YEMALIRRSL G
//
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