CAPPA_SULAC
ID CAPPA_SULAC Reviewed; 511 AA.
AC Q4JCJ1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_01904};
DE Short=PEPC {ECO:0000255|HAMAP-Rule:MF_01904};
DE Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_01904};
DE EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_01904};
GN Name=ppcA {ECO:0000255|HAMAP-Rule:MF_01904}; OrderedLocusNames=Saci_0059;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX DOI=10.1111/j.1574-6968.1997.tb10477.x;
RA Sako Y., Takai K., Nishizaka T., Ishida Y.;
RT "Biochemical relationship of phosphoenolpyruvate carboxylases (PEPCs) from
RT thermophilic archaea.";
RL FEMS Microbiol. Lett. 153:159-165(1997).
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:0000255|HAMAP-Rule:MF_01904, ECO:0000269|Ref.2}.
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:0000255|HAMAP-Rule:MF_01904, ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01904, ECO:0000269|Ref.2};
CC Note=Mg(2+) cannot be replaced by Mn(2+). {ECO:0000255|HAMAP-
CC Rule:MF_01904, ECO:0000269|Ref.2};
CC -!- ACTIVITY REGULATION: Allosterically inhibited by L-aspartate and L-
CC malate. PEPC activity is not affected by allosteric activators of
CC E.coli PEPC such as glucose 6-phosphate, fructose 1,6-bisphosphate, and
CC acetyl coenzyme A. {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.20 mM for phosphoenolpyruvate {ECO:0000269|Ref.2};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. Is extremely thermostable.
CC No loss of activity is observed after incubation for 2 hours at 80
CC degrees Celsius. The times required for 50% loss of activity are
CC about 60 minutes at 90 degrees Celsius, 10 minutes at 95 degrees
CC Celsius, and 1 minute at 100 degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01904,
CC ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the PEPCase type 2 family. {ECO:0000255|HAMAP-
CC Rule:MF_01904}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY79488.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000077; AAY79488.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_015385346.1; NC_007181.1.
DR AlphaFoldDB; Q4JCJ1; -.
DR SMR; Q4JCJ1; -.
DR STRING; 330779.Saci_0059; -.
DR EnsemblBacteria; AAY79488; AAY79488; Saci_0059.
DR GeneID; 3472974; -.
DR KEGG; sai:Saci_0059; -.
DR PATRIC; fig|330779.12.peg.55; -.
DR eggNOG; arCOG04435; Archaea.
DR HOGENOM; CLU_517433_0_0_2; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IDA:UniProtKB.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Allosteric enzyme; Carbon dioxide fixation; Lyase; Magnesium;
KW Reference proteome.
FT CHAIN 1..511
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000309614"
SQ SEQUENCE 511 AA; 58355 MW; 1337C9AF4012A917 CRC64;
MRKIPRTMST QHPDNAKVPE WNQGEAISGE NEIIEAYLAF SRYGVEEVMW DAEGKDVDTH
VVRKLLSQYP EFFRHRILGK DIFLTYRVPN PKIEGAERKV FAETLNTIPI TYDLAEKFYG
ENPNPPVFEV ILPFTTSYEE LIAVIKFYEK VIVNSDNTKL VDDTYVKDII GETNPKKIEV
IPLIEDRDSM LRIDTIVGKY IEIERPPYLR VFLARSDPAM NYGLLSAVLS VKYALSRLSK
MEKIYGVKIF PLLGVGSLPF RGHFSPYNVE NTLNEYRGIY TFTVQSAFKY DYEDDLVISA
IKKVNGTNVT EKIELSEEDE EIISNVTRKY TQGYQNKIEA LADVINKVAL LLPRRRARKL
HIGLFGYSRS TGKVTLPRAI SFVGSLYTIG IPPEIIGLSS LSKMTDQELN AIFNNYKYLK
NDLQFAARFV NFEALQLLKD IWNIDAEVVK AIKEDIDYAE NSLGIRIGES DYMSKKHVLL
STLALLSIKE GKLDEAKTYI KEMAIVRRAI G
