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Database: UniProt/TrEMBL
Entry: G8RHD5_MYCRN
LinkDB: G8RHD5_MYCRN
Original site: G8RHD5_MYCRN 
ID   G8RHD5_MYCRN            Unreviewed;       929 AA.
AC   G8RHD5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   28-MAR-2018, entry version 40.
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   OrderedLocusNames=MycrhN_5330 {ECO:0000313|EMBL:AEV75805.1};
OS   Mycobacterium rhodesiae (strain NBB3).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV75805.1, ECO:0000313|Proteomes:UP000005442};
RN   [1] {ECO:0000313|EMBL:AEV75805.1, ECO:0000313|Proteomes:UP000005442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB3 {ECO:0000313|EMBL:AEV75805.1,
RC   ECO:0000313|Proteomes:UP000005442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA   Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL   Submitted (DEC-2011) 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: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}.
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DR   EMBL; CP003169; AEV75805.1; -; Genomic_DNA.
DR   RefSeq; WP_014213546.1; NC_016604.1.
DR   STRING; 710685.MycrhN_5330; -.
DR   EnsemblBacteria; AEV75805; AEV75805; MycrhN_5330.
DR   KEGG; mrh:MycrhN_5330; -.
DR   PATRIC; fig|710685.3.peg.5355; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; MRHO710685:G1H0U-5258-MONOMER; -.
DR   Proteomes; UP000005442; 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:UP000005442};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946754};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AEV75805.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005442}.
FT   ACT_SITE    159    159       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    591    591       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   929 AA;  102908 MW;  26907D38478F46E2 CRC64;
     MAEVGGLEPI GAVQRTKVGR EATEPMREDI RLLGTILGET VREQNGEAVF ELVERARVES
     FRVRRSEIDR AELASMFDGI DIHQAIPVIR AFTHFALLAN VAEDIHRERR RVIHVAAGEP
     PQDSSLAATY AKLDTARLDA ATVSDALAGA LVSPVITAHP TETRRRTVFD TQHRITELMR
     LRMKGHEHTD DGRGIERELR RNILTLWQTA LIRLSRLKIQ DEIETGLRYY AAAFFEVVPR
     VNAEVRNALR YRWPDTDLLA EPILRPGSWI GGDRDGNPNV TAEVVRLATG SAAYTALEHY
     FTEITALEEE LSMSARLVKI SDALTALADQ CREPARADEP YRRALRAIHA RLTTTAYDIL
     DRQPEHELDL GLDRYDTPAE LLADLDVVDE SLRTNGSAVL ADDRLARLRE AVHVFGFHLS
     GLDMRQNSEV HEEVIAELLA WAGVHPDYAS LSEPDRVELL AAEVATRRPL TSDGAELSEL
     ARKELDIVAA AARAVRVLGP AAVPNYVISM CQSVSDMLEV AVLLKEVGLL DVSGSQAYAP
     VRIVPLFETI DDLQRGSSIL EQALDLPVYR ALVSARGDSQ EVMLGYSDSN KDGGYLAANW
     ALYRAELDLV ESARKTGIRL RLFHGRGGTV GRGGGPSYDA IRAQPPGAVR GSLRITEQGE
     VIAAKYAEPQ IAHRNLETLL AATLEASLLD IEGLGDAAGP AYDVLDDIAA RAQRSYAELV
     HETPGFVEYF KASTPVSEIG ALNIGSRPTS RKPTTSISDL RAIPWVLAWS QSRVMLPGWY
     GTGTAFEDWI NQGDGRLEVL RDLYQRWPFF RTVLSNMAQV LAKSDMGLAA HYSELVDDTE
     LRRRVFDKIV AEHTRTIRMH KLITGQDDLL ADNPALARSV FNRFPYLEPL NHLQVELLRR
     YRSGDDDELV QRGILLTMSG LATALRNSG
//
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