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Database: UniProt
Entry: A0A1I2MZE9_9BACL
LinkDB: A0A1I2MZE9_9BACL
Original site: A0A1I2MZE9_9BACL 
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
//
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