ID A0A0A7KLJ2_9DEIO Unreviewed; 393 AA.
AC A0A0A7KLJ2;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Aminotransferase V {ECO:0000313|EMBL:AIZ45408.1};
GN ORFNames=QR90_10360 {ECO:0000313|EMBL:AIZ45408.1};
OS Deinococcus radiopugnans.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=57497 {ECO:0000313|EMBL:AIZ45408.1, ECO:0000313|Proteomes:UP000030634};
RN [1] {ECO:0000313|Proteomes:UP000030634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY59 {ECO:0000313|Proteomes:UP000030634};
RA Jung H.-Y., Kim M.K., Srinivasan S., Lim S.;
RT "Hymenobacter sp. DG25B genome submission.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50, ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236,
CC ECO:0000256|RuleBase:RU004075}.
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DR EMBL; CP010028; AIZ45408.1; -; Genomic_DNA.
DR RefSeq; WP_039684355.1; NZ_CP010028.1.
DR AlphaFoldDB; A0A0A7KLJ2; -.
DR STRING; 1182571.QR90_10360; -.
DR KEGG; dsw:QR90_10360; -.
DR HOGENOM; CLU_027686_1_1_0; -.
DR Proteomes; UP000030634; Chromosome.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:AIZ45408.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000030634};
KW Transferase {ECO:0000313|EMBL:AIZ45408.1}.
FT DOMAIN 45..291
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 208
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 393 AA; 41494 MW; BF59F01263A4EE42 CRC64;
MTQPAPSPQT TAQPAAHVPL NRPRLIAPGP VEVDPRVLLE LAQPQMHHRS RDAVDKLMEA
REKLSRLLGD PYEAVITTSS GTGAFEGALV STTPAGARVV NAQAGKFSER WGDMARRFGY
DVGIVARPWG ELLDADAIAE ASRDAHTLLI THSETSTGAL HDLEAIARAA KAQNPDLIVI
ADCVTSYGVA ELRPAAWGVD VVVSGSQKGT ATPPGLGFVL FGPEVQARMI QNTGHGYYLD
LTRELRGQKA GNTPQTPAIN LIYALSAALD RPLSVPLDVL WAEQKRKTDA LIAAGTVLGC
PSWTARPSPA VAVLKAPEGL TGRQIAAALT GLGQRALAGQ APHEDTVFRV STMGYADRYD
ALGVAGMLED AFASLDHTFE RGAAVSAAWA ALK
//
