ID L0JHI8_NATP1 Unreviewed; 349 AA.
AC L0JHI8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Natpe_1093 {ECO:0000313|EMBL:AGB31005.1};
OS Natrinema pellirubrum (strain DSM 15624 / CIP 106293 / JCM 10476 / NCIMB
OS 786 / 157).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=797303 {ECO:0000313|EMBL:AGB31005.1, ECO:0000313|Proteomes:UP000010843};
RN [1] {ECO:0000313|Proteomes:UP000010843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 / JCM 10476 / NCIMB 786
RC {ECO:0000313|Proteomes:UP000010843};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL Submitted (FEB-2012) 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}.
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DR EMBL; CP003372; AGB31005.1; -; Genomic_DNA.
DR RefSeq; WP_015298797.1; NC_019962.1.
DR AlphaFoldDB; L0JHI8; -.
DR STRING; 797303.Natpe_1093; -.
DR GeneID; 14334256; -.
DR KEGG; npe:Natpe_1093; -.
DR eggNOG; arCOG04273; Archaea.
DR HOGENOM; CLU_017584_3_2_2; -.
DR OrthoDB; 39225at2157; -.
DR Proteomes; UP000010843; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
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; PTHR42885; HISTIDINOL-PHOSPHATE AMINOTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR42885:SF1; THREONINE-PHOSPHATE DECARBOXYLASE; 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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:AGB31005.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 23..338
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 37765 MW; 7522F691E86E94BB CRC64;
MDSDAIRRGE RVPHGGETDR DLLDFSANTN PRTPDGVADV YTAALEDSRR YPDDDYPDFR
AAAGEFVGCE PERVFPTPGG LAAIRLAMET VLEPGDEALV PYPSFGEYAR EVRLQGAAPR
FVRYDDLLDL GPTTLEPCAL AVVCTPNNPT GDAVDPAALE SFAARCAETD TTLLVDEAFL
GFTDRPSMGR LDRENVVVAR SLTKLFGLPG LRAGFAVASG DRRDALETAR RSWSLGTPAA
RVGTHCLRQD GFVRDTRERV ADERDRLREA LGERFDVHPS EAPYLLCDVG DRDVATVIAD
ARAAGVAVRD ATTFRGLDSH VRVAVKDRAA NDQLLSALGV RDADEGGDD
//
