ID   Y6286_MYCS2             Reviewed;         428 AA.
AC   A0R5R7; I7GAH4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Putative aminotransferase MSMEG_6286/MSMEI_6121;
GN   OrderedLocusNames=MSMEG_6286, MSMEI_6121;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [4]
RP   PUPYLATION AT LYS-339, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=20094657; DOI=10.1039/b916104j;
RA   Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V.,
RA   Barry C.E. III, Bark S., Dorrestein P.C.;
RT   "Expansion of the mycobacterial 'PUPylome'.";
RL   Mol. Biosyst. 6:376-385(2010).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; CP000480; ABK71113.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42552.1; -; Genomic_DNA.
DR   RefSeq; WP_011731178.1; NZ_SIJM01000013.1.
DR   RefSeq; YP_890505.1; NC_008596.1.
DR   AlphaFoldDB; A0R5R7; -.
DR   SMR; A0R5R7; -.
DR   STRING; 246196.MSMEI_6121; -.
DR   PRIDE; A0R5R7; -.
DR   EnsemblBacteria; ABK71113; ABK71113; MSMEG_6286.
DR   EnsemblBacteria; AFP42552; AFP42552; MSMEI_6121.
DR   GeneID; 66737567; -.
DR   KEGG; msg:MSMEI_6121; -.
DR   KEGG; msm:MSMEG_6286; -.
DR   PATRIC; fig|246196.19.peg.6123; -.
DR   eggNOG; COG1167; Bacteria.
DR   OMA; AMDGVAT; -.
DR   OrthoDB; 1024978at2; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR024551; AspAT_Ic.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF12897; Asp_aminotransf; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Isopeptide bond; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..428
FT                   /note="Putative aminotransferase MSMEG_6286/MSMEI_6121"
FT                   /id="PRO_0000396113"
FT   BINDING         37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..105
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         222..225
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         256..258
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        339
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000269|PubMed:20094657"
SQ   SEQUENCE   428 AA;  46411 MW;  8B733A0C565FE156 CRC64;
     MSFQSLGRDD LLAQHELQQR NYAELQAKQL KLDLTRGKPS PEQLDLSNGL LSLPGDGADA
     YRDGHGTDTR NYGGVQGLPE LRAIFAELLG LPVENLIAGN NASLEMMHDS VVFSLLHGGL
     DSPRPWSAEP TVKFLCPAPG YDRHFAITES FGIENVPVPI REDGPDVDVI EQLVASDPTI
     KGIWCVPVYS NPTGATYSTD VIRRLVQMPT AAKDFRLMWD NAYAVHTLTD EFVEPVDVLG
     LAAAAGNPNR PLVFASTSKI TFAGAGVSFL GASADNIAWY LKHAGKKSIG PDKVNQLRHL
     RFFGDADGVR RQMQRHRELI APKFALVAEI LEDRLGESKI ASWTDPKGGY FVSLDVWPGT
     AKRTVALAKD AGIAVTEAGS AFPYRKDPED KNIRIAPTFP SLPDVRDAID GLATCALLAA
     TEALLGDK