ID   L0I9Y4_HALRX            Unreviewed;       455 AA.
AC   L0I9Y4;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=4-aminobutyrate aminotransferase family protein {ECO:0000313|EMBL:AGB16390.1};
GN   OrderedLocusNames=Halru_1791 {ECO:0000313|EMBL:AGB16390.1};
OS   Halovivax ruber (strain DSM 18193 / JCM 13892 / XH-70).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Halovivax.
OX   NCBI_TaxID=797302 {ECO:0000313|EMBL:AGB16390.1, ECO:0000313|Proteomes:UP000010846};
RN   [1] {ECO:0000313|Proteomes:UP000010846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18193 / JCM 13892 / XH-70
RC   {ECO:0000313|Proteomes:UP000010846};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Halovivax ruber XH-70.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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; CP003050; AGB16390.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0I9Y4; -.
DR   STRING; 797302.Halru_1791; -.
DR   KEGG; hru:Halru_1791; -.
DR   eggNOG; arCOG00915; Archaea.
DR   HOGENOM; CLU_016922_10_0_2; -.
DR   OrthoDB; 7184at2157; -.
DR   Proteomes; UP000010846; Chromosome.
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; PTHR43206:SF2; 4-AMINOBUTYRATE AMINOTRANSFERASE GABT; 1.
DR   PANTHER; PTHR43206; 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   Aminotransferase {ECO:0000313|EMBL:AGB16390.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010846};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGB16390.1}.
FT   REGION          96..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  49562 MW;  0928D07C801592AC CRC64;
     MDRDTVEPSV ETMPGPRAEK WADYHHQFSA PSTYVYDFVW DTSAPATGPF CTDVDGNVLL
     DFTSHVAAAP LGYNNPTLRK KLDEFDLPDP TKIAGQDFYV SSDWPPEDSD QPGPTELMDR
     LTDLTSHYDM DTVFLSNSGA EAVENAIKIC YTRGGHRGVT TEGAFHGRTL GALSLNRSKT
     VQRKGYPEIP GVISIPYPST DEAYEQRWQT DGPGGNVLAD KLHPKQGVID ADELAYVILE
     PVQGEGGYRP AHPEFARDLQ ALRERYDVAV IADEIQSGMG RTGKMWGVDH LDLTPDVITS
     AKGLRVGATI SRSDVFPEET GRISSTWGAG DLLASFQGAL TIDIIQEQNL LENVQARGRQ
     LRETVVDANL PGVTDVRGPG LMIGVEFDEK ERREAVVKAA LERGLLTLGC GHRTVRLLPP
     LDVTEREIDI AADLFEAAAE AADRSVTPAA TDGGQ
//