ID A0A095Y981_9BACT Unreviewed; 397 AA.
AC A0A095Y981;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=HMPREF1640_01720 {ECO:0000313|EMBL:KGF18990.1};
OS Prevotella sp. S7-1-8.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1284775 {ECO:0000313|EMBL:KGF18990.1, ECO:0000313|Proteomes:UP000029597};
RN [1] {ECO:0000313|EMBL:KGF18990.1, ECO:0000313|Proteomes:UP000029597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7-1-8 {ECO:0000313|EMBL:KGF18990.1,
RC ECO:0000313|Proteomes:UP000029597};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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}.
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:KGF18990.1}.
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DR EMBL; JRNC01000009; KGF18990.1; -; Genomic_DNA.
DR RefSeq; WP_036891778.1; NZ_JRNC01000009.1.
DR AlphaFoldDB; A0A095Y981; -.
DR eggNOG; COG0436; Bacteria.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000029597; 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 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:KGF18990.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029597};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KGF18990.1}.
FT DOMAIN 32..389
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 397 AA; 43321 MW; ECC5AF363CB26E6C CRC64;
MAQLSDRLNS LAASATLAMS QKSAEMRARG IDVINMSVGE PDFNTPAHIK AAGIKAIEDN
CSKYSPVPGF LSLREAISDK LKRENHLQYG ANEIFVSTGG KQAVCNTVLA LVNPGDEVVI
PAPYWVSYPQ MVKIAGGEPV VIRALFERDF KITPEQLRQA ITPKTKMVIL CSPNNPTGTV
YTRDELDELA KVVLGHDGVF VLSDEIYERV NYAGANASIA SCPGMKARTI ICNGVSKAYA
MTGWRLGWAA APEWIIKGIN KLQGQYTSGT CDVSQMAALE AYNGDQACVE GMRQTFRRRR
DLIVKLAQDV PGLEVNVPQG AFYLFPKCDY FFGKSDGERA INDSADFAMY LLEEAHVATV
AGEAFGEPSG LRLSYATSDE NIREAMRRVK EAVGKLK
//
