ID A0A1I2MZE9_9BACL Unreviewed; 394 AA.
AC A0A1I2MZE9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=SAMN02982927_00192 {ECO:0000313|EMBL:SFF96974.1};
OS Sporolactobacillus nakayamae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=269670 {ECO:0000313|EMBL:SFF96974.1, ECO:0000313|Proteomes:UP000198752};
RN [1] {ECO:0000313|EMBL:SFF96974.1, ECO:0000313|Proteomes:UP000198752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700379 {ECO:0000313|EMBL:SFF96974.1,
RC ECO:0000313|Proteomes:UP000198752};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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|ARBA:ARBA00007441,
CC ECO:0000256|RuleBase:RU000481}.
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DR EMBL; FOOY01000003; SFF96974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2MZE9; -.
DR STRING; 269670.SAMN02982927_00192; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000198752; 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; ASPARTATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
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:SFF96974.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:SFF96974.1}.
FT DOMAIN 31..385
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 394 AA; 43083 MW; 7414B3DE23DFE613 CRC64;
MQLAKRVESI TPSSTLAITA KAGELKAQGY DVIGLGAGQP DFNTPKFIID AAMEAANAGH
TKYTPTAGLP ELKEAIIGKL KRDQGFNYDK SQIIVGNGAK HVLYLLFQAL LNPGDEVIIP
APYWVSYPEQ VKLAGGVPVT ITTTEEKHFK IRVEDLEQVV TSRTKALILS SPSNPTGMIY
SKEELESIAA FCIAHDILIV SDEIYEKLVY NGNVFYSIAQ ISEEVQAHTV IINGVSKSHS
MTGWRIGYAA GDQVLIKAMT NVASHSTSNP ASVSQYATIA AYNGPQESIE TMRQAFEKRL
NTIFPRLSEL PGITCVKPQG AFYLFPNIRK MSESCGFAHV SDWVTALLDE EKVAVVPGAG
FGMPDFIRLS YATSLENLEN ALDRIEHFIQ KHIN
//