ID   I3WHS4_BIFBI            Unreviewed;       516 AA.
AC   I3WHS4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   ORFNames=BBB_0844 {ECO:0000313|EMBL:AFL04437.1};
OS   Bifidobacterium bifidum BGN4.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=484020 {ECO:0000313|EMBL:AFL04437.1, ECO:0000313|Proteomes:UP000006173};
RN   [1] {ECO:0000313|EMBL:AFL04437.1, ECO:0000313|Proteomes:UP000006173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGN4 {ECO:0000313|EMBL:AFL04437.1,
RC   ECO:0000313|Proteomes:UP000006173};
RX   PubMed=22887663; DOI=10.1128/JB.00988-12;
RA   Yu D.S., Jeong H., Lee D.H., Kwon S.K., Song J.Y., Kim B.K., Park M.S.,
RA   Ji G.E., Oh T.K., Kim J.F.;
RT   "Complete Genome Sequence of the Probiotic Bacterium Bifidobacterium
RT   bifidum Strain BGN4.";
RL   J. Bacteriol. 194:4757-4758(2012).
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; CP001361; AFL04437.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3WHS4; -.
DR   SMR; I3WHS4; -.
DR   KEGG; bbf:BBB_0844; -.
DR   PATRIC; fig|484020.3.peg.833; -.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   Proteomes; UP000006173; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 1.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
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   Pfam; PF01381; HTH_3; 1.
DR   SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006173};
KW   Transferase {ECO:0000313|EMBL:AFL04437.1}.
FT   DOMAIN          15..56
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
FT   REGION          59..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   516 AA;  57389 MW;  E49EA8094994FF83 CRC64;
     MNARHLRQVD IVRAAQASGV KLGKSHISQY VSGKTTPRAD TLRFLADTLQ VDEQWLLGHD
     RGRPDMPAQP KRVSDNPGGR ADAPRTPSPQ TPSSQAPAPQ TTSPSHEPEG TPMRHFNKST
     KLDNVLYDVR GPVVDEAARM EQSGMHVLKL NIGNPAPFGF RTPDEVVYDM SRQLSDTEGY
     SASKGLFSAR KAIMQYAQLK NLPNVGIEDI YTGNGVSELI NLSLSALLDN GDEVLVPSPD
     YPLWTACVNL AGGTAVHYVC DEESEWYPDI DDMRSKITDR TVAIVLINPN NPTGALYPKE
     VLQQIVDLAR EHQLMIFSDE IYDRLVMDGL QHVSIASMAP DLFCVTFSGL SKSHMIAGYR
     IGWMVLSGNK SIAKDYVEGI NMLTNMRICS NVPAQSIVQT ALGGHQSVND YIVPGGRLYE
     QREYIYNALN SIPGVTAVKP KAAFYIFPKL DVKKFNITDD EQFALDLLHD KRILITRGGG
     FNWHEPDHFR IVYLPRIEVL KDATEKLTDF LSCYRQ
//