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Database: UniProt
Entry: G8RM51_MYCRN
LinkDB: G8RM51_MYCRN
Original site: G8RM51_MYCRN 
ID   G8RM51_MYCRN            Unreviewed;       461 AA.
AC   G8RM51;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000313|EMBL:AEV71149.1};
GN   OrderedLocusNames=MycrhN_0511 {ECO:0000313|EMBL:AEV71149.1};
OS   Mycolicibacterium rhodesiae (strain NBB3) (Mycobacterium rhodesiae).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710685 {ECO:0000313|EMBL:AEV71149.1, ECO:0000313|Proteomes:UP000005442};
RN   [1] {ECO:0000313|EMBL:AEV71149.1, ECO:0000313|Proteomes:UP000005442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB3 {ECO:0000313|EMBL:AEV71149.1,
RC   ECO:0000313|Proteomes:UP000005442};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A.,
RA   Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of Mycobacterium rhodesiae NBB3.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP003169; AEV71149.1; -; Genomic_DNA.
DR   RefSeq; WP_014208969.1; NC_016604.1.
DR   AlphaFoldDB; G8RM51; -.
DR   STRING; 710685.MycrhN_0511; -.
DR   KEGG; mrh:MycrhN_0511; -.
DR   PATRIC; fig|710685.3.peg.514; -.
DR   eggNOG; COG0161; Bacteria.
DR   HOGENOM; CLU_016922_4_0_11; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000005442; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AEV71149.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005442};
KW   Transferase {ECO:0000313|EMBL:AEV71149.1}.
SQ   SEQUENCE   461 AA;  50214 MW;  D168A09E8F22BCB6 CRC64;
     MTATDITQDI SAELGATADR HLWGHFARHG AGITPPIITR GEGVTIWDSK GKSYIDGLSG
     LFVVQVGHGR KELAEAAAKQ AETLAFFPLW SYATPPAIEL SERIAGYAPG DLNRVFFTTG
     GGEAVESAWK LAKNYFKLTG KPGKHKVISR AIAYHGTPQG ALAITGLPAF KEQFEPLTPG
     GFRAPNTNFY RAPALYEHDA KAFGQYCADR IAEAIEFEGP DTVCAVFLEP VQNAGGCFPP
     PPGYFERVRE ICDEYDVLLV SDEVICAYGR IGSMFACDDF GYVPDIITCA KGLTSGYSPI
     GAMIASDRLF EPFNDGKTTF AHGYTFGGHP VSSAVALANL DIFEREGLNA HVKEMAPAFR
     STLEQLYDLP IVGDVRGEGF FYGIELVKDK TTKETFNDEE SERLLRGFLT PALFEAGLYC
     RADDRGDPVV QLAPPLISGQ REFDAIYQIL RGVLDEASRM L
//
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