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Entry: C8WQK0_ALIAD
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Original site: C8WQK0_ALIAD 
ID   C8WQK0_ALIAD            Unreviewed;       906 AA.
AC   C8WQK0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-SEP-2017, entry version 61.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   OrderedLocusNames=Aaci_2136 {ECO:0000313|EMBL:ACV59145.1};
OS   Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC
OS   27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 /
OS   104-1A) (Bacillus acidocaldarius).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=521098 {ECO:0000313|EMBL:ACV59145.1, ECO:0000313|Proteomes:UP000001917};
RN   [1] {ECO:0000313|Proteomes:UP000001917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 /
RC   NRRL B-14509 / 104-1A {ECO:0000313|Proteomes:UP000001917};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Ovchinnikova G., Chertkov O., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete chromosome of Alicyclobacillus acidocaldarius subsp.
RT   acidocaldarius DSM 446.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595, ECO:0000256|SAAS:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; CP001727; ACV59145.1; -; Genomic_DNA.
DR   RefSeq; WP_012811406.1; NC_013205.1.
DR   STRING; 521098.Aaci_2136; -.
DR   EnsemblBacteria; ACV59145; ACV59145; Aaci_2136.
DR   KEGG; aac:Aaci_2136; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000001917; 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_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001917};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ACV59145.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ACV59145.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001917}.
FT   ACT_SITE    141    141       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    565    565       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   906 AA;  103282 MW;  875DC36A6B3FB0BC CRC64;
     MANDAPLHRD IRVLGDLLGE VLVEQCGRRV FDHVESIRLA AKAFRADPSP ETRAALQAAV
     SAVEPEHRND VIHAFSVYFQ LVNLAEQNHR LRRHRDYDRS QQVLRGSFRE TMRTLADRGM
     TADDIESLLR EVGIELVLTA HPTEALRRTV LDKHTKIAAF LEDMDDPRKT PRELDVLRER
     IRTEIVALWQ TRSVRKQRIT VLDEVRNGLY FLDQILFDVL PRVHQKLEQA VEEQFGRQLL
     ELPPLIRFGS WMGGDRDGNP NVTSDITWQT LVLHCDLALN KYEQKLRELG RDLSVSVDRA
     GADEDLLASL GGENDEPYRA LINRMLERLA NTRRRLHGER VDGPDYASPE AMMEDVERMA
     RSLAHHRGQR MVDAWLRPFL LQLRIFGFHM VTLDIRQHSG VHEQAVAELL QTAGLVDDYT
     SLGEEERVRV LSECLASPRP IRNPYHVYSD VTTEALAVLD CVRRGHETFG PRCVQDYLIS
     MTQGASDLLE VLLLAKESGL FGWPDGPMAP PKSDLNVVPL FETIEDLESA AGIMRSLFEN
     PVYRRHLEMR GWQQEIMLGY SDSNKDGGYL TANWSLYMAQ KHLIRLAEAY GVRIKFFHGR
     GGALGRGGGP VEQSILAQPT EALRGHVKIT EQGEVISQRY GHPGIAERSL ESSAAAVLVG
     ATREDSEEWA ERHPRWFRLL DRASEISFRA YRKLVFEHPA FLEYFHRATP IDEIGKMNIG
     SRPSRRSQSA RIEDLRAIPW VFSWTQSRHL LPAWYGFGSA IEAIMREDPR ALEDLRRMYE
     VWPFFRTLVD NLQMALAKAD MLVAKEYAQL AGEAGEAVFP LIEEEYARTE RAVLDITGYR
     QLLDNRPVIR ESISLRNPYV DPLSFFQVRL LADLRTDNLS PEEREAELAD ALQTINGIAA
     GLRNTG
//
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