ID A1UH65_MYCSK Unreviewed; 353 AA.
AC A1UH65;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:ABL92173.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:ABL92173.1};
GN OrderedLocusNames=Mkms_2979 {ECO:0000313|EMBL:ABL92173.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL92173.1};
RN [1] {ECO:0000313|EMBL:ABL92173.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL92173.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003693};
CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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DR EMBL; CP000518; ABL92173.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UH65; -.
DR STRING; 189918.Mkms_2979; -.
DR KEGG; mkm:Mkms_2979; -.
DR HOGENOM; CLU_017584_3_3_11; -.
DR OrthoDB; 9809616at2; -.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR PANTHER; PTHR43643:SF3; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ABL92173.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003693}; Transferase {ECO:0000313|EMBL:ABL92173.1}.
FT DOMAIN 29..338
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 353 AA; 37715 MW; 46ADDFB499346107 CRC64;
MTIVAEPGPA TSPPGPVQPR ISSLPTAVDP MALSLNENPF PPLPAVQTAM IESIQAANRY
PEFLPESLRH LIADHVAVPD EQVVVGAGAT GVLVQVMHAF TSPGDRIVLP VPTFEGYTIA
SAMTRLQVEA VPLLADGHHD LDAMADAASG ARLVVVCRPH NPTGTVESAA TLEAFLARLS
SDTIVILDEA YVEFVAPQWR IDAVDLIQRF PNVLVLRTFS KAYGLAGLRI GYAIGSWGLT
AELWAMQLPF GMGSTGLVAV AASYQAESQL RQRIRLITSE RRHLRMRLRA MGVPSIDGHA
NFVYLPVGDR PWREVFDGAD GVRVKHCADG GVRITVGGRS STGAVLAALR GRG
//
