ID I7BS33_NATSJ Unreviewed; 457 AA.
AC I7BS33;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=2,4-diaminobutyrate 4-transaminase {ECO:0000313|EMBL:AFO55585.1};
GN OrderedLocusNames=NJ7G_0332 {ECO:0000313|EMBL:AFO55585.1};
OS Natrinema sp. (strain J7-2).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=406552 {ECO:0000313|EMBL:AFO55585.1, ECO:0000313|Proteomes:UP000006507};
RN [1] {ECO:0000313|EMBL:AFO55585.1, ECO:0000313|Proteomes:UP000006507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J7-2 {ECO:0000313|EMBL:AFO55585.1,
RC ECO:0000313|Proteomes:UP000006507};
RX PubMed=22911826; DOI=10.1371/journal.pone.0041621;
RA Feng J., Liu B., Zhang Z., Ren Y., Li Y., Gan F., Huang Y., Chen X.,
RA Shen P., Wang L., Tang B., Tang X.F.;
RT "The complete genome sequence of Natrinema sp. J7-2, a haloarchaeon capable
RT of growth on synthetic media without amino acid supplements.";
RL PLoS ONE 7:E41621-E41621(2012).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP003412; AFO55585.1; -; Genomic_DNA.
DR RefSeq; WP_014862782.1; NC_018224.1.
DR AlphaFoldDB; I7BS33; -.
DR STRING; 406552.NJ7G_0332; -.
DR GeneID; 13352591; -.
DR KEGG; nat:NJ7G_0332; -.
DR PATRIC; fig|406552.5.peg.285; -.
DR eggNOG; arCOG00915; Archaea.
DR HOGENOM; CLU_016922_10_0_2; -.
DR OrthoDB; 6534at2157; -.
DR Proteomes; UP000006507; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00610; OAT_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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR004637; Dat.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00709; dat; 1.
DR PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 49025 MW; 5B191A37761B82B4 CRC64;
MTDGGSSAER LLAQQARRES NARTYPRSLP LAIERAEGAI IESVDGDEYV DCLAGAGTLA
LGHNHPAVVE RMEDLLERGR AVHTLDLTTP VKERFVDRLL ESLPDEFAEN ARVQFCSPAG
TDAVEAALKV VKTATGNRSM LAFQGGYHGM TNGALGLMGD TAAKEPVPGL MPDVHHLPYP
YEFRCPFGLG DEDCWRTSAE YVERTLSNPE SGIVDPAGMI LEPVQGEGGA VPAPAEWLRE
MRRLTRERDV PLIVDEIQTG LGRTGELYGI EHADIVPDVM TLSKAIGGGL PLSVVVYDES
LDVWEPGAHA GTFRGNQLGM AAGTATIEYV LEHDLEDHAA AMGDRLRDHL SETAATFDVV
GDVRGRGLML GMELVDPDGE PDSLGRFPAD GDLASAVQSA AFDRGLIVET GGRDGSVVRF
LPPLTISASR IDQIGDIVRE SIRATVADDH DRTEAPV
//
