ID   D1AAX5_THECD            Unreviewed;       431 AA.
AC   D1AAX5;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACY98918.1};
GN   OrderedLocusNames=Tcur_3380 {ECO:0000313|EMBL:ACY98918.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 /
OS   KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY98918.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACY98918.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC   NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP001738; ACY98918.1; -; Genomic_DNA.
DR   RefSeq; WP_012853702.1; NC_013510.1.
DR   AlphaFoldDB; D1AAX5; -.
DR   STRING; 471852.Tcur_3380; -.
DR   KEGG; tcu:Tcur_3380; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   OrthoDB; 3699548at2; -.
DR   Proteomes; UP000001918; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:ACY98918.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW   Transferase {ECO:0000313|EMBL:ACY98918.1}.
SQ   SEQUENCE   431 AA;  45902 MW;  157F70E009F27F27 CRC64;
     MSDLLARHRA VMPNWMALYY ERPIEIVSGK GVRVTDAEGN TYLDFFAGII TNILGYDVEE
     VRQAVERQLA TGVVHTSTAY LLRGQVELAE KIVALSGIKD AKVFFVNSGT EANETALLLA
     TYARKSNQVL AMRQSYHGRS FGAIGVTANR SWKNNAYTPL TVHFLHGGDR HLPQFAHLSD
     ADFIKVCTED LRHVLATATG GDVAALIAEP IQGVGGFTMP PDGLYAAYKE VLDEYGALFI
     SDEVQTGWGR TGQSFFGIHN HGVTPDIMTF AKGLGNGFAV GGVVARGDLM DAPHATGLST
     FGGNPIAMAA ANATLDYILD HDLQSNAARQ GALLLDGLKE AAPRLPVVGA VRGKGLMFAV
     ELVEPGTGEP SPPLAAAVME ETRKRGLLVG KGGLYGNVIR MAPPLTITEE DAREGLGILI
     DSLEAVSEAA K
//