(data stored in ACNUC1104 zone)

SWISSPROT: D7A341_STAND

ID   D7A341_STAND            Unreviewed;       674 AA.
AC   D7A341;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   OrderedLocusNames=Snov_0426 {ECO:0000313|EMBL:ADH87759.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87759.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87759.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
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:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-
CC         phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-
CC         phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776;
CC         EC=2.2.1.1; Evidence={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:SAAS01133303}.
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DR   EMBL; CP002026; ADH87759.1; -; Genomic_DNA.
DR   STRING; 639283.Snov_0426; -.
DR   EnsemblBacteria; ADH87759; ADH87759; Snov_0426.
DR   KEGG; sno:Snov_0426; -.
DR   eggNOG; ENOG4105CV1; Bacteria.
DR   eggNOG; COG0021; LUCA.
DR   HOGENOM; HOG000225954; -.
DR   KO; K00615; -.
DR   OMA; YALQQTD; -.
DR   BioCyc; SNOV639283:G1GLM-431-MONOMER; -.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   CDD; cd02012; TPP_TK; 1.
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;
DR   PRODOM; D7A341.
DR   SWISS-2DPAGE; D7A341.
KW   Calcium {ECO:0000256|RuleBase:RU004996};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   Magnesium {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS01130536};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS01130540};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS01133301};
KW   Transferase {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00460013}.
FT   DOMAIN       29     49       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
SQ   SEQUENCE   674 AA;  72850 MW;  D8EC257C025EB7F2 CRC64;
     MLTRNAPTSQ RPPQDLPEVL HDDMANALRA LAMDAVEQAK SGHPGMPMGM ADVATALFSR
     FVKIDPTRPD WYDRDRVVLS AGHGSMLLYA VNHLLGYADM GTDQLRRFRQ LGAVTAGHPE
     HGHTLGVETT TGPLGQGLAT AVGMALAERM LNARFGDDLV DHYTYVIAGD GCLMEGISHE
     AIDLAGHLKL GKLILLWDDN GISIDGRTTL STSTDQLARF EAAGWDVMRV DGHAYHAVTD
     AIAEARGTER PTLIACRTTI GFGAPTKAGT EGAHGAPLGP DEIAGARARL GWSHPPFEVP
     DDVREAWAHT AARGRTAREA WERRLSGSGR RAAFEAAMEG ELPADFDEKL DAYKRELSQS
     APKVATRKAS EMALGVINAE TELTVGGSAD LTHSNLTYTK GLMPVTPGNF AGRYLHYGIR
     EHAMAAVMNG LALHRGTIPY GGTFLVFSDY ARGAMRLSAL MGQRVVYVLT HDSIGLGEDG
     PTHQPVEHLA MLRATPNLHV FRPADAVETL EAWQLALHAE RTPSVLALSR QNLPTFRTTH
     SEENLTGYGA YVARKPERRR DVTLLATGSE VELAFKAADM LALRGVDAAV VSMPCWELFE
     KQSADYRRAV LGTAPRVAVE AAARFGWDRW IGERGRFVGM EGFGASAPAA DLYRYFNITP
     EAVVAAACDL ITCA
//

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