ID   A9WPD0_RENSM            Unreviewed;       405 AA.
AC   A9WPD0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=RSal33209_1148 {ECO:0000313|EMBL:ABY22886.1};
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS   NBRC 15589 / NCIMB 2235).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Renibacterium.
OX   NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY22886.1, ECO:0000313|Proteomes:UP000002007};
RN   [1] {ECO:0000313|Proteomes:UP000002007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC   {ECO:0000313|Proteomes:UP000002007};
RX   PubMed=18723615; DOI=10.1128/JB.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
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; CP000910; ABY22886.1; -; Genomic_DNA.
DR   RefSeq; WP_012244572.1; NC_010168.1.
DR   AlphaFoldDB; A9WPD0; -.
DR   SMR; A9WPD0; -.
DR   STRING; 288705.RSal33209_1148; -.
DR   KEGG; rsa:RSal33209_1148; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_11; -.
DR   Proteomes; UP000002007; Chromosome.
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; 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:ABY22886.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002007};
KW   Transferase {ECO:0000313|EMBL:ABY22886.1}.
FT   DOMAIN          65..385
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   405 AA;  45085 MW;  A5CD6F46C11D8ACB CRC64;
     MAKFSQSAKL SSVRYDVRGP ILARAQQLEA EGHRILKLNL GNPAPFGFEA PDAIFVDMIR
     HLPHAQGYSD SRGIFSARTA VVKYYQTRGI QNIDVDDVYL GNGVSELIAM SLQALLNDGD
     EILIPAPDYP LWTACVSLSG GHPVHYLCDE EADWQPDLED LEAKITPRTR GIVIINPNNP
     TGAVYPQKTV EAMVELVRKH GLIVFSDEIY EKILYEDAVH YNTALAARDD VLCLTFSGLS
     KAYRVCGYRS GWMTISGPKK AAADYLEGIN LLSNMRLCAN VPAQHAIQTA LGGYQSINDL
     ILPGGRFREQ RDLAYKLINE IPGVSTRQAQ GALYLFPKLD PEAYPIKDDE KFVLDLLQEQ
     KILVTHGSGF NWINTDHFRL VTLPNIRDLT DAIGRIAEFL SHYKP
//