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-MAR-2024, entry version 57.
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; Thermoproteota; 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-carbon
CC dicarboxylic acid source for the tricarboxylic acid cycle.
CC {ECO:0000256|HAMAP-Rule:MF_01904}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01904};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01904};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01904}.
CC -!- SIMILARITY: Belongs to the PEPCase type 2 family. {ECO:0000256|HAMAP-
CC Rule:MF_01904}.
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DR EMBL; CP001731; ADB85873.1; -; Genomic_DNA.
DR RefSeq; WP_012712741.1; NC_013769.1.
DR AlphaFoldDB; D2PDY7; -.
DR SMR; D2PDY7; -.
DR GeneID; 8759908; -.
DR KEGG; sii:LD85_0069; -.
DR HOGENOM; CLU_517433_0_0_2; -.
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 NCBIfam; TIGR02751; PEPCase_arch; 1.
DR Pfam; PF14010; PEPcase_2; 1.
DR PIRSF; PIRSF006677; UCP006677; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_01904};
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
//
