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Database: UniProt
Entry: A0A0R2TDT1_9GAMM
LinkDB: A0A0R2TDT1_9GAMM
Original site: A0A0R2TDT1_9GAMM 
ID   A0A0R2TDT1_9GAMM        Unreviewed;       384 AA.
AC   A0A0R2TDT1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=ABR85_03710 {ECO:0000313|EMBL:KRO83666.1};
OS   OM182 bacterium BACL3 MAG-120619-bin3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; OMG group; OM182 clade.
OX   NCBI_TaxID=1655593 {ECO:0000313|EMBL:KRO83666.1, ECO:0000313|Proteomes:UP000051242};
RN   [1] {ECO:0000313|EMBL:KRO83666.1, ECO:0000313|Proteomes:UP000051242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BACL22 MAG-120619-bin3 {ECO:0000313|EMBL:KRO83666.1};
RA   Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA   Andersson A.F.;
RT   "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL   Submitted (OCT-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:KRO83666.1}.
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DR   EMBL; LICD01000016; KRO83666.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2TDT1; -.
DR   Proteomes; UP000051242; 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; 3.40.640.10; 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   PANTHER; PTHR46383:SF2; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383; 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:KRO83666.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KRO83666.1}.
FT   DOMAIN          30..379
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   384 AA;  42417 MW;  6EC8616168E44EBE CRC64;
     MQPRAALASV TPFRVMSVMQ RAHELERAGK DIVHLEVGEP DFSTAQPIID AGKAALDAGR
     TQYTAATGLE ALRNKISERY RKQHGLEISP ERILITPGAS GGLLLLAHLL VGQGDGILIT
     DPAYPCVRNF IKLRDASPQL VPVVRAQAYQ PSVDDLIAQR TDITRGVWLA SPNNPTGTIL
     DRAQLEALST WTRREGLHLL VDEIYHGLHF VDDLPSVLEV DDSAFVVNSF SKYFGMTGWR
     LGWIVVPDAF IETARTLAQN MYISASSLAQ YAALAAFDPA TEVILESRRQ EFRRRRDYMV
     EELTALGFVL PEEIAGAFYV YADCSKFSND SEDFCRRMLE EHGVAMTPGT DFGDASARTM
     LRLSFTTSMA QLQVAIARLR AALA
//
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