ID D6APD6_STRFL Unreviewed; 430 AA.
AC D6APD6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:EFE75632.2};
GN ORFNames=SSGG_02999 {ECO:0000313|EMBL:EFE75632.2};
OS Streptomyces filamentosus NRRL 15998.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=457431 {ECO:0000313|EMBL:EFE75632.2, ECO:0000313|Proteomes:UP000003986};
RN [1] {ECO:0000313|Proteomes:UP000003986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RA Molnar K.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000003986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15998 {ECO:0000313|Proteomes:UP000003986};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces roseosporus strain NRRL 15998.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; DS999644; EFE75632.2; -; Genomic_DNA.
DR AlphaFoldDB; D6APD6; -.
DR Proteomes; UP000003986; Unassembled WGS sequence.
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: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; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:EFE75632.2};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:EFE75632.2}.
SQ SEQUENCE 430 AA; 45807 MW; 174A6E610F70C00E CRC64;
MESHEMHPST RTSSLWRPWT PITQQAGSLR IVEALGNRVR DVEGNWYLDG ISGVLNASCG
HGHPRLIEAA TQQLQRLVHY DPMVSSHDPA ETLAARLAEL LPGDLNETVL LNSGSEATEA
ALRIALQYWR NLGEHRDRVI TFEAAYHGTT FLAQQLSKLP FTVSEWTPPF PIEHVALPAA
PRELRTEEGA DALIAAFAQA LEAGPPAAAV MVEPLLGLGG CVVLPAGFLA RLRELCDRHG
ALLILDEVFC GFGRTGRMFG FEHEGITPDL VTMSKGISGG YVPLAAVTVT SRIKETFVRE
PVAQGLRYGH TTGGHAVASA VGNTVLDVMT DEKLVENAAA QGNALLEGLR KLEASPLITD
VRGLGLVVAI EADTPESAAA IAEASAQAGV MTRAERGVIR IAPPLTLTDD DTAEAVAKIS
GAVDVALARR
//
