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Database: UniProt
Entry: Q5NF00_FRATT
LinkDB: Q5NF00_FRATT
Original site: Q5NF00_FRATT 
ID   Q5NF00_FRATT            Unreviewed;       360 AA.
AC   Q5NF00; A0A0G2RPF4;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Sugar transamine/perosamine synthetase {ECO:0000313|EMBL:CAG46088.1};
DE            EC=4.2.1.- {ECO:0000313|EMBL:CAG46088.1};
GN   Name=wbtI {ECO:0000313|EMBL:CAG46088.1};
GN   OrderedLocusNames=FTT_1455c {ECO:0000313|EMBL:CAG46088.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG46088.1, ECO:0000313|Proteomes:UP000001174};
RN   [1] {ECO:0000313|EMBL:CAG46088.1, ECO:0000313|Proteomes:UP000001174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M., Fuxelius H.H.,
RA   Garcia E., Halltorp G., Johansson D., Isherwood K., Karp P., Larsson E.,
RA   Lui Y., Michell S., Prior J., Prior R., Sjostedt A., Svensson K.,
RA   Thompson N., Vergez L., Wagg J., Wren B., Lindler L.E., Andersson S.G.,
RA   Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR   EMBL; AJ749949; CAG46088.1; -; Genomic_DNA.
DR   RefSeq; WP_003014989.1; NZ_CP010290.1.
DR   RefSeq; YP_170392.1; NC_006570.2.
DR   AlphaFoldDB; Q5NF00; -.
DR   EnsemblBacteria; CAG46088; CAG46088; FTT_1455c.
DR   KEGG; ftu:FTT_1455c; -.
DR   PATRIC; fig|177416.36.peg.1320; -.
DR   OrthoDB; 9804264at2; -.
DR   Proteomes; UP000001174; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR30244:SF9; PROTEIN RV3402C; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:CAG46088.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001174}.
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         183
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   360 AA;  40684 MW;  540BF4512C44CFB9 CRC64;
     MSKVNVTKPY LPDINKYKSY VNKIYKNGWL TNNGPLVQEL EKRLAKYLGV KNIVLVSNGT
     IALEIAYRAL GVKGSAITTP FSFVATTSSL VSNNVKPVFV DIDENTLSID VSKIKYAIEE
     DTSAIVPVHV FGNGCEVEKI DMLAKKHNLK VIYDAAHAFD VKYKGESILN YGDISTLSFH
     ATKIFHSIEG GALIINDDSL VEKVRYFINF GIESSESIPY LGTNAKMNEF EAAMGLCVLD
     DIIEIKSKRK VITEIYEAGL DGLVKFQEQN QHSSRNYSYF PVIFRTEEEL LRVQKALIQN
     DIISRRYFYP SLDSLSYIEP KQYMPISRDI SKRILCLPIY AELEDDKINK IINNIKEVSS
//
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