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Database: UniProt
Entry: G7ZB88_AZOL4
LinkDB: G7ZB88_AZOL4
Original site: G7ZB88_AZOL4 
ID   G7ZB88_AZOL4            Unreviewed;       334 AA.
AC   G7ZB88;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative transketolase, beta-subunit {ECO:0000313|EMBL:CBS88523.1};
DE            EC=2.2.1.1 {ECO:0000313|EMBL:CBS88523.1};
GN   OrderedLocusNames=AZOLI_p10231 {ECO:0000313|EMBL:CBS88523.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p1 {ECO:0000313|EMBL:CBS88523.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS88523.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p1 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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DR   EMBL; FQ311869; CBS88523.1; -; Genomic_DNA.
DR   RefSeq; WP_014187981.1; NC_016585.1.
DR   AlphaFoldDB; G7ZB88; -.
DR   KEGG; ali:AZOLI_p10231; -.
DR   HOGENOM; CLU_009227_1_1_5; -.
DR   Proteomes; UP000005667; Plasmid AZO_p1.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 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   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Plasmid {ECO:0000313|EMBL:CBS88523.1};
KW   Transferase {ECO:0000313|EMBL:CBS88523.1}.
FT   DOMAIN          28..192
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   334 AA;  35986 MW;  4AF48D03D8F4F958 CRC64;
     MSTVANTTAK PRLKTSAMIA SIAAEGQRTK PAPFGHTLVE LAKQRPEIVG MTADLAKYTD
     LHIFAQAYPD RFYQMGMAEQ LLMGAASGMA HEGMMPFVTT YAVFASRRAY DFVHQTIAEE
     NRNVKIACAL PGLTSGYGPS HQAAEDLALF RAMPNMVVID PCDAHEIEQV VPAMAAHNGP
     VYMRLLRGNV PLVLDEYDYT FELGKAKLLR DGADVLVISS GIMTMRALEV AQRLEADKVG
     VAVLHVPTIK PLDTETILRE AGRTGRMVVV AENHTVIGGL GEAVAGTLLR GGVAPVFRQI
     GLPDEFLRAG ALPTLHDLYG ISTDAMAASI KGWL
//
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