ID A0A1M6U477_9FLAO Unreviewed; 417 AA.
AC A0A1M6U477;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Aspartate aminotransferase {ECO:0000313|EMBL:SHK63969.1};
GN ORFNames=SAMN05444371_3113 {ECO:0000313|EMBL:SHK63969.1};
OS Epilithonimonas mollis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Epilithonimonas.
OX NCBI_TaxID=216903 {ECO:0000313|EMBL:SHK63969.1, ECO:0000313|Proteomes:UP000184498};
RN [1] {ECO:0000313|Proteomes:UP000184498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18016 {ECO:0000313|Proteomes:UP000184498};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR EMBL; FRAM01000004; SHK63969.1; -; Genomic_DNA.
DR RefSeq; WP_072999776.1; NZ_FRAM01000004.1.
DR AlphaFoldDB; A0A1M6U477; -.
DR STRING; 216903.SAMN05444371_3113; -.
DR OrthoDB; 9813612at2; -.
DR Proteomes; UP000184498; 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 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; 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.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:SHK63969.1};
KW Transferase {ECO:0000313|EMBL:SHK63969.1}.
FT DOMAIN 34..404
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 417 AA; 45924 MW; D67016DD36ECA079 CRC64;
MKVSKLASNL IGSEIIKIGN EVNDLKAKGA QISNLTIGDL NSNIYPIPSE LKQGIEKAYQ
NNLTNYPPAN GLQSLRTSVS NDLKKRWNLD YSANDILITA GSRPLIYAIF KTIVDEGDKV
IYPIPSWNNN HYAYLTTANA VEVQTQESNN FLPTADDLRP YVDGAVLLCL CSPLNPTGTM
FTKEQLSEIC ELVLEENKKR GEDQKPLYLM YDQIYAMLTF GADHYNPVSL FPEMKDYTIY
VDGTSKCFAA TGVRVGWGFG PSLVIDKMKA LLTHVGAWAP KPEQEAVAEF LADNSAVDAF
LSDYKQKLNT SLKELHAGIQ ELKSKGLTVE SISPMGALYL TIKLDYLGKT APDGSKIENS
TDLVFYLINN AGMALVPFSA FGNDKSVPWF RASVGGCSLE DIKDCLPKLE KALDTLK
//
