ID A0A0F4J6F2_9ACTN Unreviewed; 612 AA.
AC A0A0F4J6F2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=VR44_25235 {ECO:0000313|EMBL:KJY28486.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY28486.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY28486.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY28486.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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|RuleBase:RU000481}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJY28486.1}.
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DR EMBL; JZWV01000726; KJY28486.1; -; Genomic_DNA.
DR RefSeq; WP_045949884.1; NZ_JZWV01000726.1.
DR AlphaFoldDB; A0A0F4J6F2; -.
DR STRING; 68223.GCA_002028425_00533; -.
DR PATRIC; fig|68223.7.peg.1142; -.
DR OrthoDB; 9788272at2; -.
DR Proteomes; UP000033551; 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:InterPro.
DR CDD; cd00609; AAT_like; 1.
DR CDD; cd02523; PC_cytidylyltransferase; 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; IPR025877; MobA-like_NTP_Trfase.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43643:SF6; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43643; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE 2; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR Pfam; PF12804; NTP_transf_3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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 Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 7..201
FT /note="MobA-like NTP transferase"
FT /evidence="ECO:0000259|Pfam:PF12804"
FT DOMAIN 303..596
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 612 AA; 66015 MW; 93DE88A8FE0C8B2D CRC64;
MNRPTKAVVL AAGLGRRLGL HHAKPLLPVA GRPILLRTLD HLAAAGVRET VLVVGYLADE
VRAAVGETHA GMAVTYVESD AYRTTNNAYS LWLAREQLDE DVYLVEGDVV FDSGLPLALA
DSGSGAEVAT AVAPYRPGMN GTVVTLGPSG TVHAMLLPAQ QGPEVDLGGT FKTANVHLLR
ARYLREEFVP ALEALIADGG HGAYYELVLA DTVTAGRFPV HAVDCAHLRW YEVDDLTDHA
AAEYLFAGSE DRLTLLEDLH GGYWRYDLVD HRLLYNLYFP PAPLVDELAR DFRDALVHYP
VGHGTLQRLL GAAIGQPAER LVVANGASEL IKILGRLAGR TALVVPGFNE YEAVFDEADV
HRIHLPAPDF TMDPAHVAGE ARRAGVGTVI ITSPNNPTSM AVPRADLVTL ARLLADAGIR
LVVDESFVDF CAPGHSLEPD LAELPGLTVV KSMSKVYGIG GLRLGYLLSA DTGFVADVRA
ALPIWNVNGF AESFLRLLPR YRDAFTASCE RVRRDRDELA ALLGELPGVT VYPPDANYVM
LRLPADTSAR EVVRRTFAEH GILVKDCGGK SMPDGDRYLR VACRGPQENR RLAEALAEVL
VGEPYPLATG AS
//
