ID   D7C636_STRBB            Unreviewed;       404 AA.
AC   D7C636;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=SBI_00903 {ECO:0000313|EMBL:ADI04024.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI04024.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI04024.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI04024.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR   EMBL; CP002047; ADI04024.1; -; Genomic_DNA.
DR   RefSeq; WP_014173503.1; NC_016582.1.
DR   AlphaFoldDB; D7C636; -.
DR   STRING; 749414.SBI_00903; -.
DR   KEGG; sbh:SBI_00903; -.
DR   PATRIC; fig|749414.3.peg.924; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0004021; F:L-alanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43488; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   PANTHER; PTHR43488:SF2; GLUTAMATE-PYRUVATE AMINOTRANSFERASE ALAA; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ADI04024.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW   Transferase {ECO:0000313|EMBL:ADI04024.1}.
FT   DOMAIN          34..391
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  45008 MW;  72A358AB02D4766E CRC64;
     MEFRQSNKLS EVCYEIRGPV IEHANALEEA GHSVLRLNTG NPALFGFEAP EEILQDMIRM
     LPQAHGYSDS RGILPARRAV VQHYQQRGLD DLGVDDVFLG NGVSELVSMA VQALVEDGDE
     ILIPAPDFPL WTAVTALAGG KPVHYVCDES ADWYPDLDDM ASKITDRTKA VVIISPNNPT
     GAVYPREILE GILDLARRHH LMVFSDEIYD KILYDGEVHH SPAVLAPDLV CLTFSGLSKA
     YRVAGFRSGW VVVSGPRQHA RNYLEGLTML ASMRLCPNTP AQFAIQAALG GRQSIEDLVL
     PGGRLHEQRD RAWEKLNEIP GVSCVKPKGA LYAFPRIDLD VHRIHDDERF VLDLLLREKI
     QVVQGTGFNW PRPDHFRILT LPHVDDLESA ISRIGRFLGG YRQS
//