ID A0A1M3EG31_9CELL Unreviewed; 378 AA.
AC A0A1M3EG31;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glutamine--scyllo-inositol aminotransferase {ECO:0000313|EMBL:OJV57220.1};
GN ORFNames=BGO38_03135 {ECO:0000313|EMBL:OJV57220.1};
OS Cellulomonas sp. 73-145.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1895739 {ECO:0000313|EMBL:OJV57220.1, ECO:0000313|Proteomes:UP000184491};
RN [1] {ECO:0000313|EMBL:OJV57220.1, ECO:0000313|Proteomes:UP000184491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=73-145 {ECO:0000313|EMBL:OJV57220.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJV57220.1}.
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DR EMBL; MKTI01000013; OJV57220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3EG31; -.
DR STRING; 1895739.BGO38_03135; -.
DR Proteomes; UP000184491; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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:OJV57220.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:OJV57220.1}.
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 378 AA; 40330 MW; DC439121FAE19098 CRC64;
MSRINVMQPW LGPEEIAAVT EVISSGWVAQ GPRVAAFEQA FAQTMDVPHA VATSSCTTAL
HLALVVAGVQ AGDEVVVPSF SFIATTNAPT YVGARPVFAD VDPVTGNLTA ETVAAVLTDR
TRAVVVVDQG GVPVDLDAIR AVTDPRGIVV VEDAACGAGS TYRGRPVGAG ADVAAWSFHP
RKIVTTGEGG MLTTPHQEWA VRARRLREHA MSVSAAARHA SVLAPPEEYL EVGYNYRMTD
LQAAVGIVQL GKLPQVVARR REIAATYAKH IADIPGLRAV ADPAWGTCNF QSFWVEVGPE
YPLDREGLLA HLADQEISAR RGIMASHRQP AYAATHHVPL PVTEHLTDTT LILPVFHQMS
ESEQHRVVDA LRSAGQSA
//
