ID L0A3Z4_DEIPD Unreviewed; 417 AA.
AC L0A3Z4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN OrderedLocusNames=Deipe_2259 {ECO:0000313|EMBL:AFZ67740.1};
OS Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416 /
OS KR-200).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ67740.1, ECO:0000313|Proteomes:UP000010467};
RN [1] {ECO:0000313|Proteomes:UP000010467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC {ECO:0000313|Proteomes:UP000010467};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Pukall R., Steenblock K., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT 19664.";
RL Submitted (MAR-2012) 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|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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DR EMBL; CP003382; AFZ67740.1; -; Genomic_DNA.
DR AlphaFoldDB; L0A3Z4; -.
DR STRING; 937777.Deipe_2259; -.
DR KEGG; dpd:Deipe_2259; -.
DR PATRIC; fig|937777.3.peg.2259; -.
DR eggNOG; COG0436; Bacteria.
DR HOGENOM; CLU_017584_4_0_0; -.
DR Proteomes; UP000010467; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR CDD; cd00609; AAT_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; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43807; FI04487P; 1.
DR PANTHER; PTHR43807:SF20; FI04487P; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000481,
KW ECO:0000313|EMBL:AFZ67740.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010467};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:AFZ67740.1}.
FT DOMAIN 53..409
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 417 AA; 44515 MW; 3263F366F82C1418 CRC64;
MSWKVGRPGL PVQPADITLA KLTGMKAIAA RVAALGPSPF AEMTALAQRY GAVNLGQGFP
DFGPPAFLQD ALLHAAMSSA HQYSPPPGLP TLREAVAEML APTLGFVADP EQEVTITVGA
TEGLAAALLA LIEPGDEVVL IEPAYDSYAP QVRMAGGTPR SVSLQRSAAG WDLPLAALQE
AGNGRTKAIV LNTPHNPTGK VFSSGELAAV AAFARQWDAY VLSDEVYDRL TFERPHVSIA
SLPDMRERTV TLGSVGKTFA ATGWRIGWAV ASPELTAALR GAHTFGPFCA PTPLQAAVAQ
GLRTAREQGY EDTMRAEYRV KRDLLTAALR AVGFEVLPCD GTFFLLADWS PFAEQAGTHD
DREFCRWLVR EVGVAAIAPS IFFSAPHRAQ GAHLARFVFC KTLSGLEEAA ARLDRLR
//
