ID   Q0RUH9_FRAAA            Unreviewed;       404 AA.
AC   Q0RUH9;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=FRAAL0078 {ECO:0000313|EMBL:CAJ58760.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ58760.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ58760.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CT573213; CAJ58760.1; -; Genomic_DNA.
DR   RefSeq; WP_011601346.1; NC_008278.1.
DR   AlphaFoldDB; Q0RUH9; -.
DR   STRING; 326424.FRAAL0078; -.
DR   KEGG; fal:FRAAL0078; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000000657; 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:CAJ58760.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW   Transferase {ECO:0000313|EMBL:CAJ58760.1}.
FT   DOMAIN          34..393
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  43880 MW;  D1099B629B67297F CRC64;
     MEFTQSDKLA DVCYDVRGPV LDEATRLEAA GARILKLNIG NPAPFGFSAP PEVLEAVVAN
     LAGAQGYSDS KGLRAAREAV VGYHNRKGIA GITPESVYLG NGVSEMIMMS LQALLNNGDE
     VLLPAPDYPL WTAVVSLCGG RPVHYLCDET AGWAPDVADI ARKVTPRTRA IVIINPNNPT
     GAVYERRVLE DIVEVARRHH LMLLSDEIYD RILYDDAEHV ATASLAPDLV CMTFNGLSKA
     YRLAGFRSGW MVLSGPRGHA SSYIEGLNIL ANMRLCANVP GQFATLAALA EDGGAGDLVL
     PGGRLREQRD TVVKLLNDIP GVSCVPPRGA LYAFPRLDPE VYPIVDDERF VFDLLAAEKI
     LLVQGTGFNW PHPDHVRIVT LPSVDDLTDA VGRIDRFLAR YKQN
//