ID K6E2Y1_9BACI Unreviewed; 451 AA.
AC K6E2Y1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Aminotransferase {ECO:0000313|EMBL:EKN67541.1};
GN ORFNames=BABA_12440 {ECO:0000313|EMBL:EKN67541.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN67541.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN67541.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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:EKN67541.1}.
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DR EMBL; AJLS01000074; EKN67541.1; -; Genomic_DNA.
DR RefSeq; WP_007085501.1; NZ_AJLS01000074.1.
DR AlphaFoldDB; K6E2Y1; -.
DR STRING; 1117379.BABA_12440; -.
DR PATRIC; fig|1117379.3.peg.2586; -.
DR eggNOG; COG0161; Bacteria.
DR OrthoDB; 9807885at2; -.
DR Proteomes; UP000006316; Unassembled WGS sequence.
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; PTHR43094; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
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:EKN67541.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000006316};
KW Transferase {ECO:0000313|EMBL:EKN67541.1}.
SQ SEQUENCE 451 AA; 49984 MW; E2E11E7C68721D80 CRC64;
MVQTSGQHET LLTQDDQYVW HSMKPYNPKT TIVAAKAEGA WVTDADGKRY LDAMAGLWCV
NVGYGRTELA EAAYEQLKEM AYFPLSQSHV PAIKLAEKLN EMLGDDYVIF FSNSGSEANE
TAFKIVRQYH QQKGESNRYK IVSRYRAYHG NSMGALAATG QAQRKYKYEP LAPGFIHVSP
PDSYRDDTNV ADPRELSSVK EIDRTMTWEL SETIAAMIME PIITGGGVLV PPDGYMKAAK
EVCEKHGALL IVDEVICGFG RTGKPFGFMN YGVKPDIITM AKGITSAYLP LSATAVRKDI
YEAFKGTEEY DYFRHVNTFG GNPAACALAL KNLEIMEKEK LFDRSRDLGE QLLNDLTNLL
QDHPYVGNIR GKGLLVGIEL VKDKTTKEPL DSGLVNQVIA SCKQEGIIIG KNGATVAGYN
NVLTLAPPLN IEQKDLQFII KTLKESLNKL L
//
