ID M8DEK1_9BACL Unreviewed; 373 AA.
AC M8DEK1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=I532_13698 {ECO:0000313|EMBL:EMT51903.1};
OS Brevibacillus borstelensis AK1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=1300222 {ECO:0000313|EMBL:EMT51903.1, ECO:0000313|Proteomes:UP000012081};
RN [1] {ECO:0000313|EMBL:EMT51903.1, ECO:0000313|Proteomes:UP000012081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EMT51903.1,
RC ECO:0000313|Proteomes:UP000012081};
RA Rajan I., PoliReddy D., Sugumar T., Rathinam K., Alqarawi S., Khalil A.B.,
RA Sivakumar N.;
RT "Assembly of a new bacterial strain Brevibacillus borstelensis AK1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|RuleBase:RU000481};
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU000481}.
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:EMT51903.1}.
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DR EMBL; APBN01000005; EMT51903.1; -; Genomic_DNA.
DR RefSeq; WP_003388902.1; NZ_APBN01000005.1.
DR AlphaFoldDB; M8DEK1; -.
DR STRING; 1300222.I532_13698; -.
DR GeneID; 72735839; -.
DR PATRIC; fig|1300222.3.peg.2864; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000012081; Unassembled WGS sequence.
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; PTHR43510; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 1.
DR PANTHER; PTHR43510:SF1; AMINOTRANSFERASE FUNCTION, HYPOTHETICAL (EUROFUNG); 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 Reference proteome {ECO:0000313|Proteomes:UP000012081};
KW Transferase {ECO:0000256|RuleBase:RU000481}.
FT DOMAIN 55..357
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 373 AA; 41751 MW; 4D333CAF42D7FED9 CRC64;
MQVKPFKVEE WMNEYEMDAV YNIAETCVDS LTVEELIRLS DEPEHFFGEL AKMKLTYGHI
EGSPEFRSLV AGLYKTMKPE NVISMNGAIG ANFLLLYSLV EPGDEVITVH PTYQQLYSVP
ESFGAQVKLL GLRPENGFYP DLGELRSMVS PKTKLICINN PNNPSGALMG EEMLREIVEI
ARSVDAYLLC DEVYRGLHQD PEAVVPSIAD LYEKGISTGS LSKVFSLAGL RLGWIAGPLD
VIKECVKHRD YNTISCGMID DVLAVHALKN YDKIMDRNLG IVRTNLQILD DWVQNEPLIS
YVKPQAGTTA MLKYELDIPS EEFCINLFKT TGAFLTPGSC FDMEGYVRIG YACATDVLRD
GLAKVSEYLR ARR
//
