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Database: UniProt
Entry: A0A0I9VH39_9MYCO
LinkDB: A0A0I9VH39_9MYCO
Original site: A0A0I9VH39_9MYCO 
ID   A0A0I9VH39_9MYCO        Unreviewed;       361 AA.
AC   A0A0I9VH39;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=ABH38_07410 {ECO:0000313|EMBL:KLO37771.1};
OS   Mycobacterium haemophilum.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO37771.1, ECO:0000313|Proteomes:UP000036334};
RN   [1] {ECO:0000313|EMBL:KLO37771.1, ECO:0000313|Proteomes:UP000036334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA   Greninger A.L., Cunningham G., Miller S.;
RT   "Genome sequence of Mycobacterium haemophilum.";
RL   Submitted (MAY-2015) 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:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KLO37771.1}.
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DR   EMBL; LDPR01000004; KLO37771.1; -; Genomic_DNA.
DR   RefSeq; WP_047314977.1; NZ_LDPT01000005.1.
DR   AlphaFoldDB; A0A0I9VH39; -.
DR   STRING; 1202450.B586_07445; -.
DR   PATRIC; fig|29311.18.peg.4448; -.
DR   OrthoDB; 9813612at2; -.
DR   Proteomes; UP000036334; Unassembled WGS sequence.
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; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR019880; OxyQ.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR03539; DapC_actino; 1.
DR   PANTHER; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42832:SF3; LL-DIAMINOPIMELATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW   ECO:0000313|EMBL:KLO37771.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036334};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000481}.
FT   DOMAIN          27..360
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   361 AA;  37618 MW;  AD5751624323DE0C CRC64;
     MSASLPVFPW DTLADAKAVA ATHPDGIVDL SVGTPVDPVA PLIQAALAAA SSAAGYPATA
     GTARLRESAV AALDRRYGIT GLTETAVLPV IGTKELIAWL PTLLGLRAGD VVVVPELAYP
     TYDVGARLAG AQVLRADSLT QLGPQSPALL YLNSPSNPTG RVLGVDHLRK VVGWARNRGV
     VVVSDECYLG LGWDAEPLSV LHPLVCDGNH AGLLAVHSLS KSSSLAGYRA GFVAGDPGLV
     AELLAVRKHA GMMVPTPVQA AMVAALEDDA HEHEQRDRYA RRRDALLPAV ASAGFTVDHS
     EAGLYLWASR GEPCRDSVVW FAARGILVAP GEFYGTGGCQ HVRVALTASD ERIAAAVARL
     S
//
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