ID A0A096BQW2_9BACT Unreviewed; 397 AA.
AC A0A096BQW2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=HMPREF2137_04355 {ECO:0000313|EMBL:KGF35619.1};
OS Hoylesella buccalis DNF00853.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=1401074 {ECO:0000313|EMBL:KGF35619.1, ECO:0000313|Proteomes:UP000029556};
RN [1] {ECO:0000313|EMBL:KGF35619.1, ECO:0000313|Proteomes:UP000029556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00853 {ECO:0000313|EMBL:KGF35619.1,
RC ECO:0000313|Proteomes:UP000029556};
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:KGF35619.1}.
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DR EMBL; JRNN01000037; KGF35619.1; -; Genomic_DNA.
DR RefSeq; WP_036872256.1; NZ_JRNN01000037.1.
DR AlphaFoldDB; A0A096BQW2; -.
DR OrthoDB; 9802328at2; -.
DR Proteomes; UP000029556; 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:KGF35619.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:KGF35619.1}.
FT DOMAIN 32..388
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 397 AA; 44003 MW; A8BA10E2E12C9BD1 CRC64;
MAHLSNRLNR LAPSATLAMS QKSSEMKAQG IDVINMSVGE PDFNTPEHIK VAAKQAIEEN
YSKYSPVPGY PDLRKAIAEK LQRENQLSYD AAEIMVSNGA KQSVCNALMA LVDDGDEVII
PAPYWVSYPQ MVKLAGGNPV IVKAGFEQNF KMTPEQLEAA ITPKTRMLIL CSPSNPTGSV
YSKEELEQLA NVIKRHEDVF VLADEIYEHI NYIGQHESIA QFPGMKERTI LVNGVSKAYA
MTGWRIGYIA APEWIVKGCN KLQGQYTSGP CSVSQRAALA AYVTEQVCVE EMRQAFQRRR
DLIVRLAKEI DGFEVNVPQG AFYLFPKCSS YFGKSDGQHT INSATDLAMY LLENGHVATV
GGDAFGDPEC IRMSYATSDE NIREALRRMK EVLAKLK
//
