GenomeNet

Database: UniProt/TrEMBL
Entry: A0A0N9XSA6_MYCFO
LinkDB: A0A0N9XSA6_MYCFO
Original site: A0A0N9XSA6_MYCFO 
ID   A0A0N9XSA6_MYCFO        Unreviewed;       934 AA.
AC   A0A0N9XSA6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-NOV-2017, entry version 15.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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:SAAS00946768};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=XA26_29140 {ECO:0000313|EMBL:ALI26749.1};
OS   Mycobacterium fortuitum.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium fortuitum complex.
OX   NCBI_TaxID=1766 {ECO:0000313|EMBL:ALI26749.1, ECO:0000313|Proteomes:UP000057134};
RN   [1] {ECO:0000313|EMBL:ALI26749.1, ECO:0000313|Proteomes:UP000057134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT6 {ECO:0000313|EMBL:ALI26749.1,
RC   ECO:0000313|Proteomes:UP000057134};
RX   PubMed=26507234; DOI=10.1128/mBio.01520-15;
RA   Costa K.C., Bergkessel M., Saunders S., Korlach J., Newman D.K.;
RT   "Enzymatic Degradation of Phenazines Can Generate Energy and Protect
RT   Sensitive Organisms from Toxicity.";
RL   MBio 6:e01520-e01515(2015).
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:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
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:SAAS00946753}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP011269; ALI26749.1; -; Genomic_DNA.
DR   RefSeq; WP_038564152.1; NZ_CP011269.1.
DR   EnsemblBacteria; ALI26749; ALI26749; XA26_29140.
DR   GeneID; 29424811; -.
DR   KEGG; mft:XA26_29140; -.
DR   PATRIC; fig|1766.6.peg.2892; -.
DR   KO; K01595; -.
DR   Proteomes; UP000057134; 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   PANTHER; PTHR30523; PTHR30523; 1.
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:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000057134};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:ALI26749.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:ALI26749.1}.
FT   ACT_SITE    161    161       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    596    596       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   934 AA;  102620 MW;  6594FC1FBC1420B2 CRC64;
     MADGPDTVLD PIGAVQRTPV GREATEPMRE DIRLLGAILG DTVREQNGDE VFDLVERARV
     ESFRVRRSEI DRAELADLFS GIDIRHAIPV IRAFTHFALL ANVAEDIHRE RRRAVHVAAG
     EPPQDSSLAA TYLKLDQADL EAAAVADALS GALVAPVITA HPTETRRRTV FDTQHRVTEL
     MRLRMHGLTH TADGRDIEVE LRRNILTLWQ TALVRLSRLK ISDEIETGLR YYPAAFFEVI
     PQVNAEVRNA LQARWPGHDL LEQPILRPGS WIGGDRDGNP NVDAGVVRLA TGRAAHVAFA
     HYFAEITALE EELSMSARLV RVSDELTALA EACGEPARAD EPYRRALRVI HGRLTATGRN
     ILDEQPEHEL DLGLDAYATP EEFLADLDTV DTSLRGHGSA VLADDRLSRL REAVRVFGFH
     LCGLDMRQNS EVHEQVVGEL LAWAGVHPDY ASLPEAKRVE LLAAEISTRR PLIGEGAELS
     ELARKELDIV GAAARAVTVF GAQAVPNYII SMCESVSDLL EAAILLKEAG LLDVSGAAHG
     EVYAPVGIVP LFETIEDLQQ GSSILEAALA LPVYRSIVTA RGQHQEVMLG YSDSNKDGGY
     LAANWALYRA ELDLVEAART TGIRLRLFHG RGGTVGRGGG PSYDAILAQP PGAVNGSLRI
     TEQGEVIAAK YAEPRIAHRN LETLLAATLE STLLDVEGLG DEAGPAYQVL DELAALAQRA
     YSELVHETPG FVDYFKASTP VSEIGALNIG SRPSSRKPTT SIADLRAIPW VLAWSQSRVM
     LPGWYGTGTA FQQWIADDET RLAVLQDLYR RWPFFRTVLS NMAQVLAKSD MGLAARYSEL
     VEDKELRARV FDKIVTEHTR TIEMYKLITG QDDLLADNPA LARSVFNRFP YLEPLNHLQV
     ELLRRYRGGD TDERVQRGIL LTMSGLATAL RNSG
//
DBGET integrated database retrieval system