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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//