ID A0A1G2DYA4_9BACT Unreviewed; 422 AA.
AC A0A1G2DYA4;
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=A2175_01035 {ECO:0000313|EMBL:OGZ18559.1};
OS Candidatus Nealsonbacteria bacterium RBG_13_42_11.
OC Bacteria; Candidatus Nealsonbacteria.
OX NCBI_TaxID=1801663 {ECO:0000313|EMBL:OGZ18559.1, ECO:0000313|Proteomes:UP000176755};
RN [1] {ECO:0000313|EMBL:OGZ18559.1, ECO:0000313|Proteomes:UP000176755}
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:OGZ18559.1}.
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DR EMBL; MHLY01000012; OGZ18559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2DYA4; -.
DR STRING; 1801663.A2175_01035; -.
DR Proteomes; UP000176755; 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 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 422 AA; 48356 MW; DD9ADDDB36D906CC CRC64;
MNQIKPISIS LSPNTQPDDI RLAFGLKFKP CKWREGKEID ELENQFKNYL GVKYAASFNS
GRSSLMAILN ALELEKGSEV LLQAFTCNAA ANPIIWSGLN PVYVDVNEQT FNIDSEDLRR
KISAKSRVVI VQHTFGLPAE MDEIAEICQE HNLILIEDCA HSLGAEYSPP HQNSGGGGKG
KKIGTFGKAA FFSFSRDKVI SSVYGGMVTT NSDELARKIR EYQERIGFPS YCWIAQQLLH
PVLMNWLILP TYRPLGKYLL VMLQRLHILS KAVHWKEKRG RIPGYFPRRL PNALATLGLN
QFKKLEKFNR HRKEIAEFYR QELKNTRLEL SPEREQIYLR FTVKHPKAHE IIRKAWNSNI
LIGDWYTTAL APYDTELERM QYVMGSCPAA EKLAEETLNL PTHINITEEE ARRVVGFLKQ
WS
//