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Database: UniProt/SWISS-PROT
Entry: CAPPA_CLOPE
LinkDB: CAPPA_CLOPE
Original site: CAPPA_CLOPE 
ID   CAPPA_CLOPE             Reviewed;         537 AA.
AC   Q8XLE8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   07-JUN-2017, entry version 87.
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};
GN   OrderedLocusNames=CPE1094;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A.,
RA   Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic
RT   flesh-eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND CRYSTALLIZATION.
RC   STRAIN=13 / Type A;
RX   PubMed=19923749; DOI=10.1107/S1744309109042663;
RA   Dharmarajan L., Kraszewski J.L., Mukhopadhyay B., Dunten P.W.;
RT   "Expression, purification and crystallization of an archaeal-type
RT   phosphoenolpyruvate carboxylase.";
RL   Acta Crystallogr. F 65:1193-1196(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:0000255|HAMAP-Rule:MF_01904, ECO:0000269|PubMed:19923749}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000255|HAMAP-Rule:MF_01904,
CC       ECO:0000269|PubMed:19923749}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01904};
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000269|PubMed:19923749}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01904}.
DR   EMBL; BA000016; BAB80800.1; -; Genomic_DNA.
DR   RefSeq; WP_011010232.1; NC_003366.1.
DR   PDB; 3ODM; X-ray; 2.95 A; A/B/C/D/E/F/G/H=1-537.
DR   PDBsum; 3ODM; -.
DR   ProteinModelPortal; Q8XLE8; -.
DR   SMR; Q8XLE8; -.
DR   EnsemblBacteria; BAB80800; BAB80800; BAB80800.
DR   KEGG; cpe:CPE1094; -.
DR   HOGENOM; HOG000009826; -.
DR   KO; K01595; -.
DR   OMA; PAMNYGL; -.
DR   OrthoDB; POG091H040O; -.
DR   BRENDA; 4.1.1.31; 1503.
DR   EvolutionaryTrace; Q8XLE8; -.
DR   Proteomes; UP000000818; Chromosome.
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   3D-structure; Carbon dioxide fixation; Complete proteome; Lyase;
KW   Magnesium; Reference proteome.
FT   CHAIN         1    537       Phosphoenolpyruvate carboxylase.
FT                                /FTId=PRO_0000309593.
FT   STRAND        5      8       {ECO:0000244|PDB:3ODM}.
FT   TURN         21     23       {ECO:0000244|PDB:3ODM}.
FT   HELIX        24     31       {ECO:0000244|PDB:3ODM}.
FT   HELIX        35     37       {ECO:0000244|PDB:3ODM}.
FT   STRAND       44     48       {ECO:0000244|PDB:3ODM}.
FT   STRAND       50     52       {ECO:0000244|PDB:3ODM}.
FT   HELIX        58     67       {ECO:0000244|PDB:3ODM}.
FT   TURN         68     70       {ECO:0000244|PDB:3ODM}.
FT   TURN         73     75       {ECO:0000244|PDB:3ODM}.
FT   STRAND       76     82       {ECO:0000244|PDB:3ODM}.
FT   TURN         86     88       {ECO:0000244|PDB:3ODM}.
FT   HELIX        91    112       {ECO:0000244|PDB:3ODM}.
FT   STRAND      119    124       {ECO:0000244|PDB:3ODM}.
FT   HELIX       128    148       {ECO:0000244|PDB:3ODM}.
FT   STRAND      157    164       {ECO:0000244|PDB:3ODM}.
FT   HELIX       167    171       {ECO:0000244|PDB:3ODM}.
FT   HELIX       174    186       {ECO:0000244|PDB:3ODM}.
FT   STRAND      192    200       {ECO:0000244|PDB:3ODM}.
FT   HELIX       201    207       {ECO:0000244|PDB:3ODM}.
FT   HELIX       209    230       {ECO:0000244|PDB:3ODM}.
FT   STRAND      233    239       {ECO:0000244|PDB:3ODM}.
FT   HELIX       244    246       {ECO:0000244|PDB:3ODM}.
FT   HELIX       254    260       {ECO:0000244|PDB:3ODM}.
FT   TURN        261    263       {ECO:0000244|PDB:3ODM}.
FT   STRAND      266    269       {ECO:0000244|PDB:3ODM}.
FT   HELIX       271    275       {ECO:0000244|PDB:3ODM}.
FT   HELIX       279    292       {ECO:0000244|PDB:3ODM}.
FT   HELIX       293    295       {ECO:0000244|PDB:3ODM}.
FT   HELIX       303    335       {ECO:0000244|PDB:3ODM}.
FT   STRAND      356    358       {ECO:0000244|PDB:3ODM}.
FT   HELIX       361    365       {ECO:0000244|PDB:3ODM}.
FT   HELIX       371    378       {ECO:0000244|PDB:3ODM}.
FT   HELIX       391    400       {ECO:0000244|PDB:3ODM}.
FT   HELIX       405    407       {ECO:0000244|PDB:3ODM}.
FT   HELIX       410    421       {ECO:0000244|PDB:3ODM}.
FT   HELIX       423    432       {ECO:0000244|PDB:3ODM}.
FT   HELIX       436    444       {ECO:0000244|PDB:3ODM}.
FT   TURN        449    455       {ECO:0000244|PDB:3ODM}.
FT   HELIX       458    474       {ECO:0000244|PDB:3ODM}.
FT   HELIX       481    487       {ECO:0000244|PDB:3ODM}.
FT   HELIX       489    506       {ECO:0000244|PDB:3ODM}.
FT   HELIX       509    514       {ECO:0000244|PDB:3ODM}.
FT   HELIX       516    533       {ECO:0000244|PDB:3ODM}.
SQ   SEQUENCE   537 AA;  60494 MW;  BCDD97C4E8EC8B8F CRC64;
     MKIPCSMMTQ HPDNVETYIS IQQEPAEAIK GLTPQDKGGL GIEEVMIDFE GKLTPYHQTS
     QIALGLISNG IIPGKDVRVT PRIPNANKES VFRQLMSIMS IIETNVQSKE LTGTPAISEV
     VVPMIETGKE ISEFQDRVNS VVDMGNKNYK TKLDLNSVRI IPLVEDVPAL ANIDRILDEH
     YEIEKSKGHI LKDLRIMIAR SDTAMSYGLI SGVLSVLMAV DGAYKWGEKH GVTISPILGC
     GSLPFRGHFS EENIDEILAT YSGIKTFTFQ SALRYDHGEE ATKHAVRELK EKIAQSKPRN
     FSEEDKDLMK EFIGICSKHY LQTFLKVIDT VSFVSDFIPK NRDRLTKAKT GLEYNREVAN
     LDNVADLVKD EVLKQEILSI DNSKEYAVPR AISFTGAMYT LGMPPELMGM GRALNEIKTK
     YGQEGIDKLL EIYPILRKDL AFAARFANGG VSKKIIDEEA RQEYKEDMKY VNEILNLGLD
     YDFLNENEFY HTLLKTTKPI IMHLMGLEEN VMRNSTEELK ILNEWIVRMG KVRGSIG
//
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