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 25-MAY-2022, entry version 101.
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=CPE1094;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; 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., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT 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-carbon
CC dicarboxylic acid source for the tricarboxylic acid cycle.
CC {ECO:0000255|HAMAP-Rule:MF_01904, ECO:0000269|PubMed:19923749}.
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,
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. {ECO:0000255|HAMAP-
CC Rule:MF_01904}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; Q8XLE8; -.
DR SMR; Q8XLE8; -.
DR STRING; 195102.gene:10490357; -.
DR EnsemblBacteria; BAB80800; BAB80800; BAB80800.
DR KEGG; cpe:CPE1094; -.
DR HOGENOM; CLU_517433_0_0_9; -.
DR OMA; QSAFRYD; -.
DR BRENDA; 4.1.1.31; 1503.
DR EvolutionaryTrace; Q8XLE8; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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; Lyase; Magnesium;
KW Reference proteome.
FT CHAIN 1..537
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000309593"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3ODM"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 24..31
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3ODM"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:3ODM"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:3ODM"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3ODM"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3ODM"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:3ODM"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 91..112
FT /evidence="ECO:0007829|PDB:3ODM"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 128..148
FT /evidence="ECO:0007829|PDB:3ODM"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:3ODM"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 209..230
FT /evidence="ECO:0007829|PDB:3ODM"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:3ODM"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:3ODM"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 303..335
FT /evidence="ECO:0007829|PDB:3ODM"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 371..378
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 391..400
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 410..421
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 423..432
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 436..444
FT /evidence="ECO:0007829|PDB:3ODM"
FT TURN 449..455
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 458..474
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 481..487
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 489..506
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 509..514
FT /evidence="ECO:0007829|PDB:3ODM"
FT HELIX 516..533
FT /evidence="ECO:0007829|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
