ID A0A1U7PIH9_9BACI Unreviewed; 394 AA.
AC A0A1U7PIH9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=SAMN05428946_1042 {ECO:0000313|EMBL:SIT74041.1};
OS Edaphobacillus lindanitolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Edaphobacillus.
OX NCBI_TaxID=550447 {ECO:0000313|EMBL:SIT74041.1, ECO:0000313|Proteomes:UP000187550};
RN [1] {ECO:0000313|EMBL:SIT74041.1, ECO:0000313|Proteomes:UP000187550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MNA4 {ECO:0000313|EMBL:SIT74041.1,
RC ECO:0000313|Proteomes:UP000187550};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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; FTPL01000001; SIT74041.1; -; Genomic_DNA.
DR RefSeq; WP_076757262.1; NZ_FTPL01000001.1.
DR AlphaFoldDB; A0A1U7PIH9; -.
DR STRING; 550447.SAMN05428946_1042; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000187550; 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; PTHR46383:SF4; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383; ASPARTATE AMINOTRANSFERASE; 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:SIT74041.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:SIT74041.1}.
FT DOMAIN 29..373
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 394 AA; 43362 MW; 447ED1FEF3E8387D CRC64;
MKSLLNEKAV EISVPGTRVF ANKVAVLSDG INLTLGEPDF PTPEPIKEAA IAAIRENKTG
YSHNAGLQEL RESVSSFFRD EYGFYYNPAS EVLITTGASE AIDSTFRAIL REGDEVILPA
PIYSGYEPVI HLAGAKPVYL DTSRTGFLPD PAALESLITG RTKAVLLNYP SNPTGVTLEK
ELMDEIVAVL ARHDVFIISD EIYSQNTYGV PHTSFASYPQ IREKLILAHG LSKSHSMTGW
RVGFLLGPEY LIEHILKVHL SNSICVSLPS QHAAIEALDH CRTVPAMMNL EYTKRRDFVH
GRLLEMGLDV KLPSGAFYLF PSIRSTGLSS FEFAEQLLEQ QHVAVVPGSS FTGFGEGFIR
ISYATSMNNL IAAMDRMEDF LNQVNLGQSV ETSK
//