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Database: UniProt
Entry: A0A0A0DB86_9PROT
LinkDB: A0A0A0DB86_9PROT
Original site: A0A0A0DB86_9PROT 
ID   A0A0A0DB86_9PROT        Unreviewed;       366 AA.
AC   A0A0A0DB86;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=P409_05910 {ECO:0000313|EMBL:KGM35183.1};
OS   Inquilinus limosus MP06.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Inquilinus.
OX   NCBI_TaxID=1398085 {ECO:0000313|EMBL:KGM35183.1, ECO:0000313|Proteomes:UP000029995};
RN   [1] {ECO:0000313|EMBL:KGM35183.1, ECO:0000313|Proteomes:UP000029995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP06 {ECO:0000313|EMBL:KGM35183.1,
RC   ECO:0000313|Proteomes:UP000029995};
RA   Pino M., Di Conza J., Gutkind G.;
RT   "Genome sequence determination for a cystic fibrosis isolate, Inquilinus
RT   limosus.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={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:KGM35183.1}.
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DR   EMBL; JANX01000043; KGM35183.1; -; Genomic_DNA.
DR   RefSeq; WP_034832928.1; NZ_JANX01000043.1.
DR   AlphaFoldDB; A0A0A0DB86; -.
DR   OrthoDB; 9809616at2; -.
DR   Proteomes; UP000029995; 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; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43510; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 1.
DR   PANTHER; PTHR43510:SF1; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 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:KGM35183.1};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KGM35183.1}.
FT   DOMAIN          47..360
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   366 AA;  39374 MW;  51BC629BEEEA07BD CRC64;
     MRYARMPIEV ESPEEYGYGL IRFNLSESSV ADRNLSQLGL QIPDLTLLYG SHRGSEALRA
     LIAAQGPGLQ PDDVLITGGA AGALFIIATA LLGRDDHLVV VRPNYATNLE TPRAIGCAIT
     TVDLRFEDGF RIDPDAIAAA VAPRTKLISV TCPHNPTGTM CSEADLRALA DLAARTGCPL
     LVDETYRDLS FDGALPLAAT LGPHVIGVSS LSKAYGVPGI RIGWIIARDP KLQELFLAAK
     EQISICGSVV DEWIAKRILE NRAAILGPTL AEMRRRRALV AGWIAGEDRL DWVAPSGGVV
     CFPRMRAEPP GGTDAFYRRL LDVHGCYVGP GHWFEMPDTC FRLGYGWPTT AELESGLAAI
     SAALRG
//
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