ID E3I880_RHOVT Unreviewed; 360 AA.
AC E3I880;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:ADP69705.1};
DE EC=2.6.1.50 {ECO:0000313|EMBL:ADP69705.1};
GN OrderedLocusNames=Rvan_0420 {ECO:0000313|EMBL:ADP69705.1};
OS Rhodomicrobium vannielii (strain ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG
OS 4299).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Rhodomicrobium.
OX NCBI_TaxID=648757 {ECO:0000313|EMBL:ADP69705.1, ECO:0000313|Proteomes:UP000001399};
RN [1] {ECO:0000313|Proteomes:UP000001399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17100 / ATH 3.1.1 / DSM 162 / LMG 4299
RC {ECO:0000313|Proteomes:UP000001399};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP002292; ADP69705.1; -; Genomic_DNA.
DR RefSeq; WP_013418110.1; NC_014664.1.
DR AlphaFoldDB; E3I880; -.
DR STRING; 648757.Rvan_0420; -.
DR KEGG; rva:Rvan_0420; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_0_5; -.
DR OrthoDB; 9768668at2; -.
DR Proteomes; UP000001399; Chromosome.
DR GO; GO:0047310; F:glutamine-scyllo-inositol transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0080100; F:L-glutamine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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 Aminotransferase {ECO:0000313|EMBL:ADP69705.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000001399};
KW Transferase {ECO:0000313|EMBL:ADP69705.1}.
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 185
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 360 AA; 38430 MW; F3A2C0153FA5DE0F CRC64;
MIPFLDLGAA YRELKAEIDA AIHRVLDSGW YILGPEVEAF EAEWAGFCGA DHAVGVANGL
DALILALRAL DIGPGDEVIV PSNTYIATWL AVTAVGARPV PVEPDPATHN IDPARIAAAI
TPATKALLPV HLYGQPADLD PILALARQRG IAVIEDAAQA HGARYKGRRI GAHGDVVCWS
FYPGKNLGAL GDGGAITTNS ADLADRIRVL RNYGSRLKYR NEVQGANSRL DPIQAAVLRA
KLPHLDAWTD RRRAIAAAYA EGLRDSGLIL PHVPDWADPV WHLYVVRSPD RAGLQKRLAE
AGVGTLIHYP IPPHMQAAYA GLGLAPDALP LARQLAEEVL SLPMGPQLAL ADAVRVMSNV
//
