ID A0A1G2QNB1_9BACT Unreviewed; 430 AA.
AC A0A1G2QNB1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=DegT/DnrJ/EryC1/StrS aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2117_00210 {ECO:0000313|EMBL:OHA61973.1};
OS Candidatus Wildermuthbacteria bacterium GWA2_46_15.
OC Bacteria; Candidatus Wildermuthbacteria.
OX NCBI_TaxID=1802443 {ECO:0000313|EMBL:OHA61973.1, ECO:0000313|Proteomes:UP000179245};
RN [1] {ECO:0000313|EMBL:OHA61973.1, ECO:0000313|Proteomes:UP000179245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {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:OHA61973.1}.
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DR EMBL; MHTO01000025; OHA61973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2QNB1; -.
DR STRING; 1802443.A2117_00210; -.
DR Proteomes; UP000179245; Unassembled WGS sequence.
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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 2.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
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 430 AA; 48948 MW; FC63DA7D7AB9A770 CRC64;
MFDQKWPVLI SLSPNTEKDD LSLALKLLFW PWRWKTTNYH GDRISTSSLE NEFKQYLGIK
HAFTFNSGRT AWWAILKALN LKEGSEVLIQ AFTCNAVVNP VRWTGFEPVF VDINERTLNI
DPVDLERKIT SASRVVLVQH TFGLAAEMEK ILGICQRHNL VLIEDCAHSL GATDQGKRLG
TLGKAAFFSF GRDKVISSVY GGLAVTDDDE LGKKLKEFQS RLPQPSRFWI CQQLLHPVLT
NLLVIPLYGL AGMGRWLLIL LQKIGLLSKA VSGKEKRGEK TSGLLQRMPD VLILLAENQF
KKLDRFVAHQ REIARFYDEN LTNPELILPP ARSGRIYLRY PLLLKNGKTD KMLDGARRKG
IFLDDGWRKT VVTPPDTDQA KMGYRAGECP AAERTAQRIL NLPTHVKVSR EKARRIVDFL
NNYRGDQRNH
//
