ID M5J404_9LACO Unreviewed; 396 AA.
AC M5J404;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=D271_05800 {ECO:0000313|EMBL:EKW98498.1};
OS Ligilactobacillus saerimneri 30a.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1227363 {ECO:0000313|EMBL:EKW98498.1, ECO:0000313|Proteomes:UP000011912};
RN [1] {ECO:0000313|EMBL:EKW98498.1, ECO:0000313|Proteomes:UP000011912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30a {ECO:0000313|EMBL:EKW98498.1,
RC ECO:0000313|Proteomes:UP000011912};
RX PubMed=23405290;
RA Romano A., Trip H., Campbell-Sills H., Bouchez O., Sherman D.,
RA Lolkema J.S., Lucas P.M.;
RT "Genome Sequence of Lactobacillus saerimneri 30a (Formerly Lactobacillus
RT sp. Strain 30a), a Reference Lactic Acid Bacterium Strain Producing
RT Biogenic Amines.";
RL Genome Announc. 1:E00097-E00012(2013).
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}.
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:EKW98498.1}.
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DR EMBL; ANAG01000017; EKW98498.1; -; Genomic_DNA.
DR AlphaFoldDB; M5J404; -.
DR STRING; 1227363.D271_05800; -.
DR PATRIC; fig|1227363.6.peg.1136; -.
DR Proteomes; UP000011912; 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:EKW98498.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011912};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:EKW98498.1}.
FT DOMAIN 33..387
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 396 AA; 42876 MW; DCF19BC507DC421F CRC64;
MGINITDKIN AIAPSATLAL STKAKEMQAQ GIDVINLSIG EPDFNTPEHI KQAAIAAITA
GKSDFYTPAL GIKELRSAIA TKVTKMLGVP TSADQVAVTA GGKFSLYAVT QAVISAGDEV
LIPLPYWVSY GEQVKLAAGK PVFVRPTAAT GRVSVADLEA NRTDRTKLLI INSPQNPAGL
VYTREELQAI GDWAVEHDIV IIADDMYSEL IYNGNQFTSI WQLSAAIREQ TILVSGFSKT
YAMTGWRVGY TVAPQWFIKK LGSFIGHTTS NIAAVSQYAA LAAATGPQTC VEEMRLQYEQ
RLNTIYPLLS AIPGVDLRKP AGAFYMFPNV KKTATMCGYS TVSDFCTALL EQAHVAVVPG
VAFGMDEHIR LSYATSMENL MEAVKRLDKF VQQHLQ
//
