ID B2U7C3_RALPJ Unreviewed; 374 AA.
AC B2U7C3;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:ACD25785.1};
DE EC=2.6.1.50 {ECO:0000313|EMBL:ACD25785.1};
GN OrderedLocusNames=Rpic_0634 {ECO:0000313|EMBL:ACD25785.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD25785.1};
RN [1] {ECO:0000313|EMBL:ACD25785.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12J {ECO:0000313|EMBL:ACD25785.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP001068; ACD25785.1; -; Genomic_DNA.
DR AlphaFoldDB; B2U7C3; -.
DR STRING; 402626.Rpic_0634; -.
DR KEGG; rpi:Rpic_0634; -.
DR PATRIC; fig|402626.5.peg.1836; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_7_2_4; -.
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:ACD25785.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:ACD25785.1}.
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 374 AA; 40683 MW; 407A5C532B8A86A9 CRC64;
MIPFLDLKSI NARQRAELIS AFTEVLDAGW FIHGKQCEAF EADFAAYCEA KHCIGISNGL
DALHLILRAM SIGKGDEVIV PSNTFIATWL AVTFAGATPV PVEPREDTCN LDPSLIAAAI
TPRTRAIIPV HLYGQPADMD PILEIAHQHG LKVIEDAAQS HGARYRGKRT GSLGDAAAFS
FYPGKNLGAL GDGGAVTTSD TALAQRIRML SNYGSQKKYV HEAAGFNARL DEIQAAMLRA
KLVLLDADNA RRRSIADRYT RALIDCGLGL PILANDVESA WHIYAIHHPN RDALQRALSE
RGVGTVVHYP TPPHLQGAYR DLRLGEGAYP ISERIHRETL SLPMSPVMTD VQVDEVIHTV
RSVCGELAVD VTNL
//
