ID   Q3ILZ5_NATPD            Unreviewed;       440 AA.
AC   Q3ILZ5;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=Pyridoxal phosphate-dependent aminotransferase {ECO:0000313|EMBL:CAI50874.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:CAI50874.1};
GN   OrderedLocusNames=NP_6188A {ECO:0000313|EMBL:CAI50874.1};
OS   Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS   8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OG   Plasmid PL131 {ECO:0000313|EMBL:CAI50874.1,
OG   ECO:0000313|Proteomes:UP000002698}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=348780 {ECO:0000313|EMBL:CAI50874.1, ECO:0000313|Proteomes:UP000002698};
RN   [1] {ECO:0000313|EMBL:CAI50874.1, ECO:0000313|Proteomes:UP000002698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 /
RC   NCIMB 2260 / Gabara {ECO:0000313|Proteomes:UP000002698};
RX   PubMed=16169924; DOI=10.1101/gr.3952905;
RA   Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA   Oesterhelt D.;
RT   "Living with two extremes: conclusions from the genome sequence of
RT   Natronomonas pharaonis.";
RL   Genome Res. 15:1336-1343(2005).
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; CR936258; CAI50874.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3ILZ5; -.
DR   EnsemblBacteria; CAI50874; CAI50874; NP_6188A.
DR   KEGG; nph:NP_6188A; -.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   OrthoDB; 6534at2157; -.
DR   Proteomes; UP000002698; Plasmid PL131.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 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   Aminotransferase {ECO:0000313|EMBL:CAI50874.1};
KW   Plasmid {ECO:0000313|EMBL:CAI50874.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002698};
KW   Transferase {ECO:0000313|EMBL:CAI50874.1}.
SQ   SEQUENCE   440 AA;  47407 MW;  E96D2EE953D78736 CRC64;
     MSQEHSPQTT NSEIEDQYEQ YLMPIWKDLD VPIRRAEGCT VEDFDGNEYL DVFSGIAVTN
     AGHRNDAVVE AAKDQLDEFI HGCSYLHPHQ PAAELAKRLA EITPGDLEKS FFANSGTEAV
     EGAIKLARKY TGSKEVIALE MSFHGRTLGS LALTGNKGYK NEMAPTINDV AHVAPPYAYR
     CQLCDGGPCS NDCGDRLEQV IQTHTAGDLA AVVVEPVMGE GGIIVPPEGW LERVQEITHD
     HGGLLIVDEV QAGYGRTGEM WASDHFDVVP DIMPQAKGIA NGLPLGAFTA RPEIADAFES
     GDHLSTFGGN PVACAAALET IEQLEAGLID NARTQGEWLT SRLEELEADH EVIGDTRGLG
     LMQGIELIDA GGETGPMDVA PEPDAKLAKK VSHHLREEGI VIGVGGFHGN VLRFQPPLSI
     SRDQLERTVD AIDDALSAKE
//