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Database: UniProt
Entry: D1Y3C7_9BACT
LinkDB: D1Y3C7_9BACT
Original site: D1Y3C7_9BACT 
ID   D1Y3C7_9BACT            Unreviewed;       645 AA.
AC   D1Y3C7;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   07-JUN-2017, entry version 39.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:EFB91201.1};
DE            EC=2.2.1.1 {ECO:0000313|EMBL:EFB91201.1};
GN   ORFNames=HMPREF7215_0291 {ECO:0000313|EMBL:EFB91201.1};
OS   Pyramidobacter piscolens W5455.
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Pyramidobacter.
OX   NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB91201.1, ECO:0000313|Proteomes:UP000006462};
RN   [1] {ECO:0000313|EMBL:EFB91201.1, ECO:0000313|Proteomes:UP000006462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W5455 {ECO:0000313|EMBL:EFB91201.1,
RC   ECO:0000313|Proteomes:UP000006462};
RA   Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA   Sutton G.G., Strausberg R.L., Nelson K.E.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00651192};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|SAAS:SAAS00651232};
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|SAAS:SAAS00651207}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFB91201.1}.
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DR   EMBL; ADFP01000047; EFB91201.1; -; Genomic_DNA.
DR   RefSeq; WP_009164265.1; NZ_ADFP01000047.1.
DR   ProteinModelPortal; D1Y3C7; -.
DR   STRING; 352165.HMPREF7215_0291; -.
DR   EnsemblBacteria; EFB91201; EFB91201; HMPREF7215_0291.
DR   eggNOG; ENOG4105CV1; Bacteria.
DR   eggNOG; COG0021; LUCA.
DR   OrthoDB; POG091H02B4; -.
DR   BioCyc; PPIS352165-HMP:GMRO-18-MONOMER; -.
DR   Proteomes; UP000006462; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006462};
KW   Magnesium {ECO:0000256|SAAS:SAAS00651250};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00651225};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006462};
KW   Thiamine pyrophosphate {ECO:0000256|SAAS:SAAS00651235};
KW   Transferase {ECO:0000256|SAAS:SAAS00651241,
KW   ECO:0000313|EMBL:EFB91201.1}.
FT   DOMAIN      328    498       Transket_pyr. {ECO:0000259|SMART:
FT                                SM00861}.
SQ   SEQUENCE   645 AA;  68699 MW;  991C96EEE9F912AC CRC64;
     MLFDEAVKIN SFQWEKLPQA EERQLNKAAQ VCKGLAVAMV ARANSGHPAG ALSSMKMYMA
     AYGAANVSPQ NCDSLDRDFV VVSHGHTSAA AYATLAYYGF VDAFDAVNEF RRTGSRFQGH
     VERMVPGIDW GSGCLGQGLS AGAGFALAQK ARGYDGRVYV LMGDGEQPKG QIAEARRLIA
     ARKLTSVTAL IDVNDIQISG RCGDVMPAHI KELWEADGWQ TLLCDGDSFA ELYVALKAAR
     AAGRPTAILC RTTMGKGVSF MEDTPDYHGK AASGDLYRQA MKELGQPDLV ALAAEHKKAK
     FSAARAVEPL EAVLDLGAAK VYGPADTTDN RSAFGSALAE VGQLNYKKTG RAPVLVFDCD
     LAGSVKTGEF AKKCPDNFIQ CGIQENTTAT AAGAASAGGV VSVWADFGVF GLAEAYNQQR
     MNDVNRAGEK LVLTHVGLDV GEDGMTHQCI DYVSLMSNFF NWKLVVPADP NQTDRATRWA
     LKTAGNVCLA MGRSKLPALC ANGKPLLARD FTYGEAVKVR EGKDAAILAL GAMAGRAVQA
     AELLAEKGVE TAVYAVSCPL EIDERALTEA FQTGTVLTVE DHNVVSGMGS LWLARAEELG
     LHSVARRLGV HRYGDSGPSE EVYAAMGLSA DKIAESLEEL KKVAR
//
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