ID   F8B019_9ACTN            Unreviewed;       423 AA.
AC   F8B019;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, 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   OrderedLocusNames=FsymDg_4467 {ECO:0000313|EMBL:AEH11716.1};
OS   Candidatus Protofrankia datiscae.
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC   Protofrankia.
OX   NCBI_TaxID=2716812 {ECO:0000313|EMBL:AEH11716.1, ECO:0000313|Proteomes:UP000001549};
RN   [1] {ECO:0000313|EMBL:AEH11716.1, ECO:0000313|Proteomes:UP000001549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4085684 {ECO:0000313|Proteomes:UP000001549};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Chertkov O., Teshima H., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Berry A.,
RA   Pawlowski K., Persson T., Vanden Heuvel B., Benson D., Woyke T.;
RT   "Complete sequence of chromosome of Frankia symbiont of Datisca
RT   glomerata.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002801; AEH11716.1; -; Genomic_DNA.
DR   RefSeq; WP_013875561.1; NZ_CAAAGZ010000266.1.
DR   AlphaFoldDB; F8B019; -.
DR   STRING; 656024.FsymDg_4467; -.
DR   KEGG; fsy:FsymDg_4467; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   Proteomes; UP000001549; Chromosome.
DR   GO; GO:0004069; F:L-aspartate: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:AEH11716.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001549};
KW   Transferase {ECO:0000313|EMBL:AEH11716.1}.
FT   DOMAIN          34..394
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   423 AA;  45977 MW;  588912217B9551EA CRC64;
     MEFTQSDKLT GVCYDVRGPV LDQATKLEAA GQRILKLNIG NPAPFGFHAP PAVLEAVVNG
     LAEAQGYSDS KGLLSARTAA VRYANGKGIT GIDPDGVYLG NGVSELIMMS LQALLNDGDE
     VLLPAPDYPL WTAVVSLCGG RPVHYLCDES AGWMPDLDAL ASRITTRTRA IVVINPNNPT
     GAVYDREILE GIVELARQHN LMIFSDEIYD RILYDDAEHI STAALAPDVV CVTFNGLSKA
     YRLAGFRSGW MVLSGPRTHA SSYVEGLNIL ANMRLCANVP GQFAMRAALE DDSGAGDLVL
     PGGRLHEQRD VVWKLLNDIP GVSCVKPKGA LYAFPRLDPD VYPVTDDERL VLDLLLAEKI
     MVVQGTGFNW PRPDHFRIVT LPDVDDLTDA VSRISRFLTA YAQGETVHRR DGLPTFEPQH
     VPS
//