ID A0A1H5M5J6_9ACTN Unreviewed; 452 AA.
AC A0A1H5M5J6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Taurine---2-oxoglutarate transaminase {ECO:0000313|EMBL:SEE84505.1};
GN ORFNames=SAMN05216533_3945 {ECO:0000313|EMBL:SEE84505.1};
OS Streptomyces sp. Ag109_O5-10.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855349 {ECO:0000313|EMBL:SEE84505.1, ECO:0000313|Proteomes:UP000198812};
RN [1] {ECO:0000313|EMBL:SEE84505.1, ECO:0000313|Proteomes:UP000198812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag109_O5-10 {ECO:0000313|EMBL:SEE84505.1,
RC ECO:0000313|Proteomes:UP000198812};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNTQ01000001; SEE84505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5M5J6; -.
DR STRING; 1855349.SAMN05216533_3945; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000198812; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000198812}.
SQ SEQUENCE 452 AA; 48070 MW; ABC5BD2C25019660 CRC64;
MTPQPSPQAG AAVKAADRAH VFHSWSAQDL IDPLAVAGAE GSYFWDYDGR RYLDFTSGLV
FTNVGYQHPK IVAAIQEQAA RMTTFAPAFA VEARSEAARL IAERTPGDLD KIFFTNGGAD
AVEHAVRMAR LHTGRPKVLS AYRSYHGGTQ QAINLTGDPR RWASDGAAAG VVHFWAPFLY
RSRFYAETEE QETARALEHL ETTIAFEGPG TVAAIVLETI PGTAGIMVPP AGYLAGVREL
CDKYGIVFVL DEVMAGFGRT GEWFAADLFG VVPDLMTFAK GVNSGYVPLG GVAIGQKIAE
TFGKRPYPGG LTYSGHPLAC AAAVATIGVM AEEGVVENAK RLGAEVVGPA LAALAERHPC
VGEVRGVGMF WALDLVKSRE TREPLVPYNA AGEANAAMAA FGAAAKEHGL WPFVNMNRTH
VVPPCNVSEA ELKEGFAALD AALSVADRFT VA
//