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Database: UniProt
Entry: A0A0S8FG94_9GAMM
LinkDB: A0A0S8FG94_9GAMM
Original site: A0A0S8FG94_9GAMM 
ID   A0A0S8FG94_9GAMM        Unreviewed;       664 AA.
AC   A0A0S8FG94;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-APR-2018, entry version 10.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   ORFNames=AMJ59_09705 {ECO:0000313|EMBL:KPK59768.1};
OS   Gammaproteobacteria bacterium SG8_31.
OC   Bacteria; Proteobacteria; Gammaproteobacteria.
OX   NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK59768.1};
RN   [1] {ECO:0000313|EMBL:KPK59768.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_31 {ECO:0000313|EMBL:KPK59768.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur
RT   cycling among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from
CC       a ketose donor to an aldose acceptor, via a covalent intermediate
CC       with the cofactor thiamine pyrophosphate.
CC       {ECO:0000256|RuleBase:RU004996}.
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC       {ECO:0000256|RuleBase:RU004996}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|RuleBase:RU004996, 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:KPK59768.1}.
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DR   EMBL; LJTI01000017; KPK59768.1; -; Genomic_DNA.
DR   PATRIC; fig|1703405.3.peg.3324; -.
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; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; PTHR43522; 1.
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.
DR   TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|RuleBase:RU004996};
KW   Magnesium {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651250};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651225};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651235};
KW   Transferase {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651241, ECO:0000313|EMBL:KPK59768.1}.
FT   DOMAIN       12     32       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
SQ   SEQUENCE   664 AA;  72637 MW;  EC1C731C533F98C9 CRC64;
     MSDRREFANA IRALSMDAVQ AANSGHPGMP MGMADIAEVL WNDFLSHNPG NPLWPNRDRF
     VVSNGHGSML LYSLLYLSGY DVSIEELKNF RQLGFRTAGH PEYEPEMGVE TTTGPLGQGL
     TNAVGMALAE RVLAAHYNRP GHEIIDHHTY VFVGDGCLME GISHEACSLA GTLGLGKLIF
     IYDDNGISID GDVEGWFTDD TPGRFEAYGW HVVRDVDGHD VEAVGKAIEA AREEAQRPTI
     ICCKTVIGWG SPNKQGSEST HGAALGEEEV QATRDNIGWP YPPFEIPDAI RAGWDAKERG
     RQREDAWHIQ MESYASEYPE LARELQRRLR GDLPDNWQAM ADAAIGQIAE NGGDMATRKA
     SQVALEAFGP GLPELIGGSA DLTGSNNTFW SGSRTITGKE PDGNYLHFGV REFGMTAILN
     GISLHGGFKP YGGTFLVFSD YARNAVRMAA LMHQPVILVY THDSIGLGED GPTHQPVEHL
     SSLRIIPNMH VWRPCDSVES AVAWRLALES RKTPHSLVFS RQSLPFQTRD DRQIADITRG
     GYVLRDAGPD PQVILIATGS EVALAMAAAR ALEEDDLQVR VVSMPCASVF DQQDSAYRDS
     VLLPDVRKRV AIEAGVPDFW YRYVGDGGAV IGMDTFGASA PAKHLFEHFG FSVENVKKTV
     MQLG
//
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