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Database: UniProt/TrEMBL
Entry: A0A060LWA5_9BACI
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ID   A0A060LWA5_9BACI        Unreviewed;       429 AA.
AC   A0A060LWA5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:AIC95546.1};
GN   ORFNames=BleG1_2982 {ECO:0000313|EMBL:AIC95546.1};
OS   Shouchella lehensis G1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX   NCBI_TaxID=1246626 {ECO:0000313|EMBL:AIC95546.1, ECO:0000313|Proteomes:UP000027142};
RN   [1] {ECO:0000313|EMBL:AIC95546.1, ECO:0000313|Proteomes:UP000027142}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G1 {ECO:0000313|EMBL:AIC95546.1,
RC   ECO:0000313|Proteomes:UP000027142};
RX   PubMed=24811681; DOI=10.1016/j.gene.2014.05.012;
RA   Noor Y.M., Samsulrizal N.H., Jema'on N.A., Low K.O., Ramli A.N.,
RA   Alias N.I., Damis S.I., Fuzi S.F., Isa M.N., Murad A.M., Raih M.F.,
RA   Bakar F.D., Najimudin N., Mahadi N.M., Illias R.M.;
RT   "A comparative genomic analysis of the alkalitolerant soil bacterium
RT   Bacillus lehensis G1.";
RL   Gene 545:253-261(2014).
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|RuleBase:RU003560}.
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DR   EMBL; CP003923; AIC95546.1; -; Genomic_DNA.
DR   RefSeq; WP_038482527.1; NZ_CP003923.1.
DR   AlphaFoldDB; A0A060LWA5; -.
DR   STRING; 1246626.BleG1_2982; -.
DR   KEGG; ble:BleG1_2982; -.
DR   PATRIC; fig|1246626.3.peg.2972; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_9; -.
DR   OrthoDB; 9807885at2; -.
DR   Proteomes; UP000027142; 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; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:AIC95546.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027142};
KW   Transferase {ECO:0000313|EMBL:AIC95546.1}.
SQ   SEQUENCE   429 AA;  47080 MW;  B0EA65D31F8A9421 CRC64;
     MSQSWNELQE TIPYRLAPSM AKDHPNLPVV KEEGCYYYGV DGKTYLDFTS GIAVTNVGHR
     HPKVVEAIKK EADSFTHGPI GVIQYESILK LANELADVMP GDLDCFFFGN SGTEAIEGAL
     KLARHVTKRP NVVSFTGCFH GRTLGAMSVS TSKAKYRAYQ PAQNQVYQLP YYQPGESVDE
     AIAKLEKACE TMFAHYTLPE EVACFIIEPV LGEGGYIVPP AKWLQHIREI CTKHGILLIF
     DEVQTGFGRT GEWFAAQSFD VIPDIMAVAK GIASGLPLSA TVANHTLMQQ WPLGSHATTF
     GGNPIACAAA RATLQIIKEE NVLSNVKEVG SYAAEELTKL QQAYPCIGSI RHLGMMFGIE
     IVHPETGRKD GELAAQILDL ALEEGVLFYF CGNEGEVLRM IPPLTITKEQ IDEGLTKLKN
     ALQRLKEIG
//
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