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Database: UniProt
Entry: A0A0V8QE24_9FIRM
LinkDB: A0A0V8QE24_9FIRM
Original site: A0A0V8QE24_9FIRM 
ID   A0A0V8QE24_9FIRM        Unreviewed;       395 AA.
AC   A0A0V8QE24;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:KSV58802.1};
GN   ORFNames=ASU35_11495 {ECO:0000313|EMBL:KSV58802.1};
OS   Acetivibrio ethanolgignens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Acetivibrio.
OX   NCBI_TaxID=290052 {ECO:0000313|EMBL:KSV58802.1, ECO:0000313|Proteomes:UP000054874};
RN   [1] {ECO:0000313|EMBL:KSV58802.1, ECO:0000313|Proteomes:UP000054874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACET-33324 {ECO:0000313|EMBL:KSV58802.1,
RC   ECO:0000313|Proteomes:UP000054874};
RA   Zou Y., Xue W., Luo G., Lv M.;
RT   "Butyribacter intestini gen. nov., sp. nov., a butyric acid-producing
RT   bacterium of the family Lachnospiraceae isolated from the human faeces.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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:KSV58802.1}.
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DR   EMBL; LNAM01000160; KSV58802.1; -; Genomic_DNA.
DR   RefSeq; WP_058352952.1; NZ_LNAM01000160.1.
DR   AlphaFoldDB; A0A0V8QE24; -.
DR   STRING; 290052.ASU35_11495; -.
DR   OrthoDB; 9810913at2; -.
DR   Proteomes; UP000054874; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KSV58802.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054874};
KW   Transferase {ECO:0000313|EMBL:KSV58802.1}.
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         194
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   395 AA;  44727 MW;  643D2B4E8BF3EB4A CRC64;
     MGNKEHIFLA SPHMSEEGYE QEYIKEAFDT NWIAPLGKNV TEFEKEMEEK TGAKKAVALS
     SGTAAIHMAL KAIGVKEGDI IFCQSLTFAA TANPIIYEKA IPVFIDSEEE TWNMSPAALQ
     MAFEKYEKMG RLPKAVIVVH LYGISAQIEK IADICRKYKV ALVEDAAESL GTLYKGKYTG
     TFGDYGIISF NGNKIITTSG GGMLFINTKD AEKKAKKVLF WATQAREQAL WYQHEEIGYN
     YRMSNIVAGI GRGQLKILDK RVEKKRYIYD FYERKLGKIT GFHMMPKERE MDSRNNCWLT
     AVQLSGERKR PFEIIEAFKE SDIESRPIWK PLHLQPVFNH CDFITEVEKQ KIVDEKTGAD
     SSVAGNIFCN GLCLPSDTKM TDDDLERVCK VLLVE
//
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