ID A0A108T4H2_9BACE Unreviewed; 368 AA.
AC A0A108T4H2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=DegT/DnrJ/EryC1/StrS family aminotransferase {ECO:0000313|EMBL:KAA5412071.1};
GN ORFNames=F2Y81_27055 {ECO:0000313|EMBL:KAA5412071.1};
OS Bacteroides cellulosilyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=246787 {ECO:0000313|EMBL:KAA5412071.1, ECO:0000313|Proteomes:UP000448877};
RN [1] {ECO:0000313|EMBL:KAA5412071.1, ECO:0000313|Proteomes:UP000448877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A6 {ECO:0000313|EMBL:KAA5412071.1,
RC ECO:0000313|Proteomes:UP000448877};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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:KAA5412071.1}.
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DR EMBL; VVYV01000083; KAA5412071.1; -; Genomic_DNA.
DR RefSeq; WP_060408403.1; NZ_VVYV01000083.1.
DR AlphaFoldDB; A0A108T4H2; -.
DR Proteomes; UP000448877; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR CDD; cd00616; AHBA_syn; 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 PANTHER; PTHR30244:SF9; PROTEIN RV3402C; 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:KAA5412071.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Transferase {ECO:0000313|EMBL:KAA5412071.1}.
FT ACT_SITE 185
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 185
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 368 AA; 41783 MW; E624C862B9985F66 CRC64;
MENKLITVTS PLLPSLDDLF PYLQDIWNRK WLTNNGYYHQ ELERALCEYL KVPFISLFTN
GTLPLMCALQ ALRITGEVIT TPYSFIATTH SLWWNGIKPV FVDIDPETCN IDPNKIEAAI
TPKTTAIMPV HVYGKPCDIN RIQEIADKYG LKVIYDAAHA FGVEVDGRSI LEAGDLSTLS
FHATKVYNTV EGGALICHDE KTKKRIDYLK NFGFAGETEI VAPGINGKMD EIRSAYGLLN
LKQVDSAIDA RCKVAMKYRD SLRGVPGIHF MEDMPNVRHN YSYFPIFVDA EKYGMSRDEL
YFKMKQHNVL GRRYFYPLIS AFSTYRGLES AKPEGLQNSI KKANEVICLP MYHDLADEDI
ARILELIV
//
