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Database: UniProt
Entry: A0A0G1T858_9BACT
LinkDB: A0A0G1T858_9BACT
Original site: A0A0G1T858_9BACT 
ID   A0A0G1T858_9BACT        Unreviewed;       366 AA.
AC   A0A0G1T858;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-NOV-2023, entry version 29.
DE   RecName: Full=Glutamine-scyllo-inositol transaminase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UY03_C0006G0009 {ECO:0000313|EMBL:KKU77951.1};
OS   Parcubacteria group bacterium GW2011_GWA2_47_64.
OC   Bacteria.
OX   NCBI_TaxID=1618845 {ECO:0000313|EMBL:KKU77951.1, ECO:0000313|Proteomes:UP000034132};
RN   [1] {ECO:0000313|EMBL:KKU77951.1, ECO:0000313|Proteomes:UP000034132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKU77951.1}.
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DR   EMBL; LCOL01000006; KKU77951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1T858; -.
DR   PATRIC; fig|1618845.3.peg.279; -.
DR   Proteomes; UP000034132; Unassembled WGS sequence.
DR   CDD; cd00616; AHBA_syn; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 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   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}.
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         189
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   366 AA;  41290 MW;  982E3300B6D553FC CRC64;
     MIPFLNLKKN NEKYREELID AFTCVIDSGR YILGEEVRAF EWEFGTYCGV KHAIGTGNGL
     DAITLIIRAY KELGIFKEGD EILVPANTYI ATILSITENR LKPVLVEPDI RTYNLDATLL
     EKKVTSKTKA ILTVHLYGKI GYSDEMGAIA KKHGLMIIED SAQAHGAIYK GRKTGSLGDA
     SGFSFYPSKP LGALGDAGIV TTNDSKLAKV VAALRNYGSR EKYHNLSQGV NSRLDELQAA
     LLRVKLRHLD DDNQKRRKIA QRYLREIRNK KLILPEEGTP ERHVWHLFVV RTEKRDALQK
     HLSKNGIETL IHYPVPPHKQ PAFKDWNKKS YPITEEIHNT VLSLPLYSAM TKEEISIIIE
     ACNSFS
//
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