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Database: UniProt/TrEMBL
Entry: D2PDY7_SULID
LinkDB: D2PDY7_SULID
Original site: D2PDY7_SULID 
ID   D2PDY7_SULID            Unreviewed;       511 AA.
AC   D2PDY7;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-SEP-2017, entry version 42.
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   OrderedLocusNames=LD85_0069 {ECO:0000313|EMBL:ADB85873.1};
OS   Sulfolobus islandicus (strain L.D.8.5 / Lassen #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=425944 {ECO:0000313|EMBL:ADB85873.1, ECO:0000313|Proteomes:UP000001404};
RN   [1] {ECO:0000313|Proteomes:UP000001404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L.D.8.5 / Lassen #2 {ECO:0000313|Proteomes:UP000001404};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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; CP001731; ADB85873.1; -; Genomic_DNA.
DR   RefSeq; WP_012712741.1; NC_013769.1.
DR   EnsemblBacteria; ADB85873; ADB85873; LD85_0069.
DR   GeneID; 8759908; -.
DR   KEGG; sii:LD85_0069; -.
DR   HOGENOM; HOG000038601; -.
DR   KO; K01595; -.
DR   OMA; PAMNYGL; -.
DR   OrthoDB; POG093Z01LI; -.
DR   Proteomes; UP000001404; 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_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:UP000001404};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01904};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01904}.
SQ   SEQUENCE   511 AA;  58763 MW;  AEFD2C8731AB991E CRC64;
     MRIIPRTMST QHPDNAKVPE WAKSEVIEGE DEVKEAFLAY SMYGVHEVMW DAEGKDVDTH
     VVRKLLSNYP DYFREHILGK DVFLTYRLPN PKVEGADRKV FAETMESIPI TYDLAEKFYG
     NGITVPVFEV ILPMTTSNLE IISVARYYEK AVANEDELEL YDGVKVKDLV GEIYPKVIEV
     IPLVEERDSL QNIDNIVEGY YKVIKPKYMR VFLARSDPAM NYGMITAVLS VKIALSELYK
     LSESLNFEIY PIIGVGSLPF RGHLSPENYE KVLEEYKGVY TYTIQSAFKY DYDYDKVKSA
     ISSINNSRIG PAKILEKYEE DVLRKITILY TERYQPIIES LANAINDVSV LLPRRRARKL
     HIGLFGYSRS AGKVSLPRAI SFVGSLYSIG IPPELIGISS LSNLDEKEWD IFKQNYVNFK
     HDLQTAARFF NWESFELIKD IWKISEDTIA KIKEDIDYAE SVIGIKLGGI DYDSRKHILM
     SSLFLLSFKE KILQESKKYL YEMALIRRSL G
//
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