ID E0RZH6_BUTPB Unreviewed; 392 AA.
AC E0RZH6;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Aminotransferase DegT/DnrJ/EryC1/StrS family {ECO:0000313|EMBL:ADL33173.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:ADL33173.1};
GN OrderedLocusNames=bpr_I0425 {ECO:0000313|EMBL:ADL33173.1};
OS Butyrivibrio proteoclasticus (strain ATCC 51982 / DSM 14932 / B316)
OS (Clostridium proteoclasticum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=515622 {ECO:0000313|EMBL:ADL33173.1, ECO:0000313|Proteomes:UP000001299};
RN [1] {ECO:0000313|EMBL:ADL33173.1, ECO:0000313|Proteomes:UP000001299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51982 / DSM 14932 / B316
RC {ECO:0000313|Proteomes:UP000001299};
RX PubMed=20689770; DOI=10.1371/journal.pone.0011942;
RA Kelly W.J., Leahy S.C., Altermann E., Yeoman C.J., Dunne J.C., Kong Z.,
RA Pacheco D.M., Li D., Noel S.J., Moon C.D., Cookson A.L., Attwood G.T.;
RT "The glycobiome of the rumen bacterium Butyrivibrio proteoclasticus B316(T)
RT highlights adaptation to a polysaccharide-rich environment.";
RL PLoS ONE 5:E11942-E11942(2010).
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}.
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DR EMBL; CP001810; ADL33173.1; -; Genomic_DNA.
DR RefSeq; WP_013279830.1; NC_014387.1.
DR AlphaFoldDB; E0RZH6; -.
DR STRING; 515622.bpr_I0425; -.
DR KEGG; bpb:bpr_I0425; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_2_4_9; -.
DR Proteomes; UP000001299; Chromosome 1.
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; IPR026385; LegC-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04181; NHT_00031; 1.
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:ADL33173.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001299};
KW Transferase {ECO:0000313|EMBL:ADL33173.1}.
FT ACT_SITE 202
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 202
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 392 AA; 44107 MW; 0FC4A154D6318BC4 CRC64;
MDKFIPLSVP NFEGNERKYV DDAIDQGWVS TGGAYISRLE KELANFMHVE NVAACQSGTS
ALHMALVEAG VKPGDVVLVP PLTFIAAVNP VRYQFAEPVF IDCDDSFCMD PDKLRDFCQD
ECDWDGESLK HNGKEVKAIV VVHVFGNMAD MEAVMDVAST YGLKVIEDAT EALGTYYLEG
KYSGRYAGTI GNFGCFSFNG NKIITTGGGG AITANNPEVV DHIRFLSTQA KTDPHFYIHD
EIGYNYRMTN LQAALGVAQM EELPEFIKRK QKNFELYKNE FVDCKYAELM PFRVGVSSNK
WFYSLCIDRN VIITPMRDII LMLKEKGIET RAIWGLINEQ KPYLNYETYK LEKAPYYADR
ILNIPSSTSI TEDEIHYVAD EIKKLLEALV NG
//
