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Database: UniProt/TrEMBL
Entry: D7BTN2_STRBB
LinkDB: D7BTN2_STRBB
Original site: D7BTN2_STRBB 
ID   D7BTN2_STRBB            Unreviewed;       906 AA.
AC   D7BTN2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   28-MAR-2018, entry version 53.
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   ECO:0000313|EMBL:ADI07471.1};
GN   OrderedLocusNames=SBI_04351 {ECO:0000313|EMBL:ADI07471.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI07471.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI07471.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI07471.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI07471.1; -; Genomic_DNA.
DR   RefSeq; WP_014176942.1; NC_016582.1.
DR   STRING; 749414.SBI_04351; -.
DR   EnsemblBacteria; ADI07471; ADI07471; SBI_04351.
DR   KEGG; sbh:SBI_04351; -.
DR   PATRIC; fig|749414.3.peg.4497; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   BioCyc; SBIN749414:G1GKW-4355-MONOMER; -.
DR   Proteomes; UP000000377; 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:UP000000377};
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:ADI07471.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377}.
FT   ACT_SITE    132    132       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    564    564       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   906 AA;  100251 MW;  07E666B8197E8E7A CRC64;
     MSSADNTNAA LRADIRRLGD LLGETLVRQE GPDLLDLVER VRALTRSDGE AAAELLGDTD
     LETAAKLVRA FSTYFHLANI TEQVHRGREL RAKRAAEGGL LSRTADQLKD ADPEHLREAV
     RHLNVRPVFT AHPTEAARRT VLNKLRRVAE LLDTLAVGGD KRRTDLRLAE NIDLLWQTDE
     LRVARPEPAD EARNAIYYLD ELHAGAVGDV LEDLSAELER VGAPLPATTR PLTFGTWIGG
     DRDGNPNVTP QVTWDVLILQ HEHGITDALA IVDDLRAALS SSIRNSDASE ELLDSLQRDL
     ELLPEISPRY KRLNAEEPYR LKATCVRQKL LNTRTRLAGG TPHQPGRDYL GTAELLADLH
     LIQESLRAHR GRLIADGRME RAIRTLAAFG LQLATMDVRE HADAHHHALG QLFDRLGEES
     WRYADMPRDS RRKLLAKELR SRRPLAPTPA PLDAAGAKTL GVFHTISEAF ERFGPEIVES
     YIISMCQGSD DVFAAAVLAR EAGLVDLHAG WAKIGIVPLL ETTEELKIAD QLLDDMLSDP
     SYRRLVALRG DVQEVMLGYS DSSKFGGITT SQWEIHRAQR LLRDVAHRHG VRLRLFHGRG
     GTVGRGGGPT HDAILAQPWG TLEGEIKVTE QGEVISDKYL VPSLARENLE LTVAATLQAS
     ALHTAPRQSD EALAGWDAAM DTVSDAAHRA YRALVEDPDL PAYFFASTPV DQLAELHLGS
     RPSRRPDSGA GLDGLRAIPW VFGWTQSRQI VPGWFGVGSG LKAAREAGLD PALDEMHQHW
     HFFRNFLSNV EMTLAKTDLR IARHYVDTLV PDELKHVFAT IEAEHELTVR EVLRITGETE
     LLDSNPVLKQ TFHVRDAYLD PISYLQVSLL HRQRTAHEQG EAPDPLLARA LLLTVNGVAA
     GLRNTG
//
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