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Database: UniProt
Entry: A0A369R4Q9_9RHOB
LinkDB: A0A369R4Q9_9RHOB
Original site: A0A369R4Q9_9RHOB 
ID   A0A369R4Q9_9RHOB        Unreviewed;       404 AA.
AC   A0A369R4Q9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=DLJ49_00395 {ECO:0000313|EMBL:RDC75250.1};
OS   Rhodovulum sp. 12E13.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodovulum.
OX   NCBI_TaxID=2203891 {ECO:0000313|EMBL:RDC75250.1, ECO:0000313|Proteomes:UP000253860};
RN   [1] {ECO:0000313|EMBL:RDC75250.1, ECO:0000313|Proteomes:UP000253860}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12E13 {ECO:0000313|EMBL:RDC75250.1,
RC   ECO:0000313|Proteomes:UP000253860};
RA   Zhang R.;
RT   "Rhodovulum sp. nov.,isolated from saltern sediment.";
RL   Submitted (JUL-2018) 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:RDC75250.1}.
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DR   EMBL; QPLK01000001; RDC75250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369R4Q9; -.
DR   OrthoDB; 9813612at2; -.
DR   Proteomes; UP000253860; 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; PTHR42832; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42832:SF3; LL-DIAMINOPIMELATE 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:RDC75250.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253860};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000481}.
FT   DOMAIN          37..385
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   404 AA;  43649 MW;  115E00C65FEE4DDC CRC64;
     MMAPERFSDL PEYAFPRLRR LLGDRAPGRA SGAAPVDMTI GEPRHPMPAF VPDVLAREAA
     GFAKYPPNEG TPGLRGAIGE WLGRRYGVPA DPETEVQVVN GTREGLFNAA LALCPERKGG
     TPAMLIPNPF YQVYAVAALA VGAEPVYVNA TAETGFLPDF ESLPEDVLDR TAIAWLCSPS
     NPQGAVADEA YWRRLLGLAE KHDFLVFADE CYSEIWRDAP PPGAWQVAEG MGLPRERVVI
     FHSLSKRSNL PGLRAGFLAS GAANIARIRQ LRSYAGAPLP LPIQHAAEAA WRDEAHVAAS
     LALYHEKFRL ADGIWGDWPG YHAPAGGFFL WLPVPQGFAD GEAATLAAWE RAGVRVLPGT
     YLSRDTARGN PGERYVRVAM VAGADEVARG LTALREVFET EGTG
//
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