ID F7YYD5_9THEM Unreviewed; 398 AA.
AC F7YYD5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
DE Flags: Precursor;
GN ORFNames=Theth_0874 {ECO:0000313|EMBL:AEH50958.1};
OS Pseudothermotoga thermarum DSM 5069.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH50958.1, ECO:0000313|Proteomes:UP000006804};
RN [1] {ECO:0000313|EMBL:AEH50958.1, ECO:0000313|Proteomes:UP000006804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH50958.1,
RC ECO:0000313|Proteomes:UP000006804};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermotoga thermarum DSM 5069.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; CP002351; AEH50958.1; -; Genomic_DNA.
DR RefSeq; WP_013932180.1; NC_015707.1.
DR AlphaFoldDB; F7YYD5; -.
DR STRING; 688269.Theth_0874; -.
DR KEGG; tta:Theth_0874; -.
DR PATRIC; fig|688269.3.peg.898; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_3_0; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000006804; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:AEH50958.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006804};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:AEH50958.1}.
FT DOMAIN 35..341
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 398 AA; 44547 MW; C529A95B84F800E4 CRC64;
MNLSGRALTA PASPIRRMIP FAEQAMKMGK KIYYLNIGQP DIPTPRVYFE YVERYKPSVV
AYTHSAGLLE LREAFSRYYE KFSVKVLPDE IIVTNGGSEA VLFAMAVVAD PGDEILVLEP
FYANYAGFAA QLGIKLVPVR TYPEDGYSVP DKKKFLEKIS SKTKAIIFSN PCNPTGAVYN
ESQLRTIIDV ALEKDLFIIS DEVYREFTFD GCKAISALSF EPILDRVIMV DSISKRYSAC
GARIGAFVSK NKSIYSAALK FAQARLCPPM TSQYGAIGLL SLDDEYVESI KNEYQARRDV
VYEELKKIDG AVFQKPKGAF YISARLPVDN VEEFVKFMLL EFDVGGKTTM VSPLDGFYAT
PSAGLDEMRI AYVLNCDDLR DAVRILALGV EEYKRKVR
//
