ID I7A2R9_MELRP Unreviewed; 386 AA.
AC I7A2R9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:AFN75483.1};
GN OrderedLocusNames=MROS_2253 {ECO:0000313|EMBL:AFN75483.1};
OS Melioribacter roseus (strain JCM 17771 / P3M-2).
OC Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC Melioribacteraceae; Melioribacter.
OX NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN75483.1, ECO:0000313|Proteomes:UP000009011};
RN [1] {ECO:0000313|EMBL:AFN75483.1, ECO:0000313|Proteomes:UP000009011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17771 / P3M-2 {ECO:0000313|Proteomes:UP000009011};
RX PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT organotrophic bacterium representing a novel deep lineage within
RT Bacteriodetes/Chlorobi group.";
RL PLoS ONE 8:E53047-E53047(2013).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP003557; AFN75483.1; -; Genomic_DNA.
DR RefSeq; WP_014856915.1; NC_018178.1.
DR AlphaFoldDB; I7A2R9; -.
DR STRING; 1191523.MROS_2253; -.
DR GeneID; 78567176; -.
DR KEGG; mro:MROS_2253; -.
DR PATRIC; fig|1191523.3.peg.2379; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_0_10; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000009011; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009011}.
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 187
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 386 AA; 43760 MW; 5A842855ACBB60BB CRC64;
MKVPLLDLKP QYQSIKEEID RAIMKVVESQ YFILGPEVEA LEKEICDYTG AKYAVGVSSG
TDALLLSLMA LGIKSGDEVI LPTYSFFATA GVVARLDATP VFTDIDPVTF NIDVKEIEKK
ITPKTKAIIP VHLYGQSAEM DEIMEVARKH NLYVIEDGAQ AIGVQYKDGR FVGTIGHTGC
FSFFPSKNLG GFGDGGIVTT NDEEIYHRLK IMRVHGMEPK YYHKVIGGNF RLDALQAAVL
RVKLPHLDKW SEKRRANARL YYDLFEKTGL VDDKNNYLKP EKIILPEAVY KNINGLKNYH
IYNQFVIRVA NRDALLEHLK KNEIGCEVYY PVPFHRQECF AYLNAVDGDY PVSNLAAETS
LALPIYPELK EEQIEFVVRK ISEFYR
//
