ID A0A1V2M4H0_9FIRM Unreviewed; 390 AA.
AC A0A1V2M4H0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN ORFNames=AN396_13920 {ECO:0000313|EMBL:ONI42595.1};
OS Epulopiscium sp. SCG-B11WGA-EpuloA1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Candidatus Epulonipiscium.
OX NCBI_TaxID=1710701 {ECO:0000313|EMBL:ONI42595.1, ECO:0000313|Proteomes:UP000188605};
RN [1] {ECO:0000313|EMBL:ONI42595.1, ECO:0000313|Proteomes:UP000188605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCG-B11WGA-EpuloA1 {ECO:0000313|EMBL:ONI42595.1};
RA Seilhamer J.J.;
RL Submitted (AUG-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|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:ONI42595.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJDB01000010; ONI42595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2M4H0; -.
DR STRING; 1710701.AN396_13920; -.
DR Proteomes; UP000188605; 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:SF5; AMINOTRANSFERASE; 1.
DR PANTHER; PTHR46383; 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:ONI42595.1};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:ONI42595.1}.
FT DOMAIN 30..378
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 390 AA; 43165 MW; 2C666FA768C95843 CRC64;
MQDKISLKVK NMPPSGIRKF FDVASEMGDA ISLGVGEPDF DTPWHVREEA IYSLEQGKTV
YSANAGLLTL REEICKYMKR RFDLTYNPKT ETLVTVGGSE GIDVSLRTLL EAGEEVLIPE
PSFVAYMPCT IFAGGVPVPI ATKAENQFKL TADEIENAIT DKSKLLILPY PNNPTGAIME
REELEKIAKV IIKNDLIVLS DEIYAELTYG INHVSIANIE GMYERTIILS GFSKAYAMTG
WRLGYALGPP AVIQAMTKMH QYVLMCAPTT SQYGAISAMK NGDSDVREMR KAYDGRRKLM
LDGFKKMGLS CFEPKGAFYV FPSIKETGMT SEEFCEALLK EEKVAVVPGN AFGSSGEGYI
RCSYAYSIAE LKEALVRIER FVSKILASKS
//
