ID   D6CUV3_THIA3            Unreviewed;       416 AA.
AC   D6CUV3;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=alanine transaminase {ECO:0000256|ARBA:ARBA00026106};
DE            EC=2.6.1.2 {ECO:0000256|ARBA:ARBA00026106};
GN   OrderedLocusNames=THI_2443 {ECO:0000313|EMBL:CAZ89072.1};
OS   Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX   NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ89072.1, ECO:0000313|Proteomes:UP000002372};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=3As;
RA   Genoscope - CEA;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22701 / CIP 110005 / 3As
RC   {ECO:0000313|Proteomes:UP000002372};
RX   PubMed=20195515; DOI=10.1371/journal.pgen.1000859;
RA   Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M.,
RA   Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V.,
RA   Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J.,
RA   Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C.,
RA   Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P.,
RA   Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E.,
RA   Weiss S., Weissenbach J., Medigue C., Bertin P.N.;
RT   "Structure, function, and evolution of the Thiomonas spp. genome.";
RL   PLoS Genet. 6:E1000859-E1000859(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; FP475956; CAZ89072.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6CUV3; -.
DR   KEGG; thi:THI_2443; -.
DR   eggNOG; COG0436; Bacteria.
DR   HOGENOM; CLU_017584_4_2_4; -.
DR   Proteomes; UP000002372; 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:CAZ89072.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002372};
KW   Transferase {ECO:0000313|EMBL:CAZ89072.1}.
FT   DOMAIN          37..397
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   416 AA;  46150 MW;  2C3E7502A99BD0CB CRC64;
     MVVREFRKSD KLADVCYDIR GPVLDKARQM EEEGQRIIKL NIGNLAVFGF EPPDEIVQDM
     IHNLPSAAGY TDSKGLFAPR KSIVHYTQEK GIAGVSIDDV FIGNGASELI NMSMNALLNN
     GDEVLIPAPD YPLYTASVAL SGGKPVHYIC DEQSDWYPDI ADIRSKITPN TRAIVVINPN
     NPTGALYPRE LLEEIVQVAR EHELIVFADE IYDKTLYDGN THTSIASLAD DVLFITFNGL
     SKNYRSCGYR SGWMVVSGNK RCARDYIEGL TMLASMRLCA NTPGQLAIQT ALGGYQSIKD
     LVAPQGRLTK QRDLAYDLLT QIPGVSVVKP KAALYMFPRL DPEIYPIADD QQFAYDLLAQ
     EKVLIVQGTG FNWPQPDHFR LVFLPNADDL TEAIGRIARF LETLRKRSRA VASASA
//