ID A0A063ZLD2_9EURY Unreviewed; 400 AA.
AC A0A063ZLD2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Alanine--glyoxylate aminotransferase {ECO:0000313|EMBL:KDE58859.1};
GN ORFNames=EL22_01875 {ECO:0000313|EMBL:KDE58859.1};
OS Halostagnicola sp. A56.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=1495067 {ECO:0000313|EMBL:KDE58859.1, ECO:0000313|Proteomes:UP000027027};
RN [1] {ECO:0000313|EMBL:KDE58859.1, ECO:0000313|Proteomes:UP000027027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A56 {ECO:0000313|EMBL:KDE58859.1,
RC ECO:0000313|Proteomes:UP000027027};
RA Pore S.D., Kanekar S.P., Arora P., Saxena N., Dhakephalkar P.K.;
RT "Draft genome of Halostagnicola sp. A56 isolated from Andaman Islands,
RT India.";
RL Submitted (JUN-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDE58859.1}.
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; JMIP02000017; KDE58859.1; -; Genomic_DNA.
DR RefSeq; WP_050051086.1; NZ_JMIP02000017.1.
DR AlphaFoldDB; A0A063ZLD2; -.
DR STRING; 1495067.EL22_01875; -.
DR OrthoDB; 166535at2157; -.
DR Proteomes; UP000027027; Unassembled WGS sequence.
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:KDE58859.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000027027};
KW Transferase {ECO:0000313|EMBL:KDE58859.1}.
FT DOMAIN 42..343
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 400 AA; 43166 MW; 7ED4B2F81F3701BD CRC64;
MPTTDNETPD ISELTPPSRT LMGPGPSNSN PRVLRAMSTP LVGHLDPSFV EIMNDVQELL
RYTFRTDNEW TIPVSGTGSA AMEAAIGNLV EPGDTMLVPT NGYFGDRMAS MARRAGGTVV
EVDAPWGEPL ETPTVEDALE THDPDVFGFV HAETSTGVLQ PNVPELTAAA HDHEALVIAD
TVTSLGGVEL RVDEWDIDVA YAGPQKCLSC PPGASPLTLS DEAMEKVLSR EQAPRSWYLD
LSLLEGYWGD ERAYHHTAPI TNVYALREAL RLVVEEGIES RWNRHERMAG ALKAGVEAMG
LEMNAPEEYW LPSLNAVQVP DGIDNSEVCE TLLERYDLEI AGGLGDLSGE IFRIGCMGHS
ARAENVIFAV TALGDVLESL GADVDPGKGV TATRRSLATE
//
