ID U4KHJ1_9VIBR Unreviewed; 321 AA.
AC U4KHJ1;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Putative Transketolase, C-terminal subunit {ECO:0000313|EMBL:CCO61284.1};
DE EC=2.2.1.1 {ECO:0000313|EMBL:CCO61284.1};
GN ORFNames=VIBNI_B1537 {ECO:0000313|EMBL:CCO61284.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO61284.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO61284.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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DR EMBL; FO203527; CCO61284.1; -; Genomic_DNA.
DR RefSeq; WP_022561733.1; NC_022543.1.
DR AlphaFoldDB; U4KHJ1; -.
DR STRING; 28173.VIBNI_B1537; -.
DR KEGG; vni:VIBNI_B1537; -.
DR PATRIC; fig|1260221.3.peg.5132; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000016895; Chromosome 2.
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; IPR020826; Transketolase_BS.
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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCO61284.1}.
FT DOMAIN 13..178
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 321 AA; 34634 MW; 557B660672A80DC4 CRC64;
MNIETPFEPN SLVSLRDAYA KTIMSVGNAH ENVYMLDADL SKSTKTAEFA SQYPNRALNI
GIAEQNMVGI AAGLSTMGLV PFVNTFAAFL TRRACDQIAI SVAYPKLNVK FFGFHGGINL
GEDGATQQAV EDIAIMRSIP NIRVYSPIDA NDLAWVVNDI MAHEGPTYVR LSRFPSPTLL
TEKSKPKKET PAYRVMKPGS DLMVITTGTL TSKLLDAAKV MEEKGLKVQV VAVTRIKPLG
GELADIVMNT DAPVAVVEEH SIHGGLADAV SQLLDARAHS HVLHRIGVQD RFGESGHPDA
LLEAFELAGD PLVKKLSALI S
//
