ID L0I911_HALRX Unreviewed; 401 AA.
AC L0I911;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Serine-pyruvate aminotransferase/archaeal aspartate aminotransferase {ECO:0000313|EMBL:AGB16095.1};
GN OrderedLocusNames=Halru_1487 {ECO:0000313|EMBL:AGB16095.1};
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:AGB16095.1, 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-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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; AGB16095.1; -; Genomic_DNA.
DR AlphaFoldDB; L0I911; -.
DR STRING; 797302.Halru_1487; -.
DR KEGG; hru:Halru_1487; -.
DR eggNOG; arCOG00082; Archaea.
DR HOGENOM; CLU_027686_0_0_2; -.
DR OrthoDB; 166535at2157; -.
DR Proteomes; UP000010846; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd06451; AGAT_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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AGB16095.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Pyruvate {ECO:0000313|EMBL:AGB16095.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010846};
KW Transferase {ECO:0000313|EMBL:AGB16095.1}.
FT DOMAIN 46..299
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 42698 MW; CE8EC6C4DA6D68FE CRC64;
MDHHSAGEVT APAVSELDPP NRTLMGPGPS DVHPRVRRAM STPLVGHLDP SFVELMDEVQ
ELLRYTFRTE NEWTIPVSGT GSAAMEAAIG NLVEPGETML VPTNGYFGGR MAEMARRAGG
DVVEVDAPWG EPLDPADVES ALAAHDPDVF GFVHAETSTG VLQPDVPALT DAAHDHDALV
VADTVTSLGG VELRVDEWDI DVAYAGPQKC LSCPPGASPL TLSDEAMEKV LSREEAPRSW
YLDLSLLEGY WGDERAYHHT APITNVYALR EALRLVAEEG IESRWRRHER LAGALKAGVV
GMGLEMNAPD DYWLPSLNAV RVPDGVDDGE ICQTVLDDYD LEIAGGLGDL AGDIFRIGCM
GHAASPANVV LTITALGDAL ATAGADVDPD AGIGAVREAL R
//
