ID A0A1F4EYW0_9PROT Unreviewed; 368 AA.
AC A0A1F4EYW0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Aminotransferase DegT {ECO:0000313|EMBL:OGA66337.1};
GN ORFNames=A3F77_07485 {ECO:0000313|EMBL:OGA66337.1};
OS Betaproteobacteria bacterium RIFCSPLOWO2_12_FULL_67_28.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1797503 {ECO:0000313|EMBL:OGA66337.1, ECO:0000313|Proteomes:UP000177406};
RN [1] {ECO:0000313|EMBL:OGA66337.1, ECO:0000313|Proteomes:UP000177406}
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:OGA66337.1}.
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DR EMBL; MERO01000123; OGA66337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4EYW0; -.
DR STRING; 1797503.A3F77_07485; -.
DR Proteomes; UP000177406; 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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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:OGA66337.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:OGA66337.1}.
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 368 AA; 40112 MW; BE65ADD1778F2587 CRC64;
MDFIDLKSQY AAMRDIINAR IQLVLDHGQY ILGPEVRELE DRLAAYTGAK HCITVASGTE
ALLIALMALG VKPGDEVITS PFTFVATAEM VVLLGATPVF VDVEEDTANI SAARIEAAIS
ARTRAILPVS LYGQPADMDQ INAIAAKHRL PVIEDAAQSF GATYKGAKSG NLSTIGCTSF
FPSKPLGCYG DGGALFTQDD ALAKAMREIR IHGQERRYVH TRIGVGGRMD SIQCAVVLAK
LKRFDWEIER RIEIGNHYNA TLSRHMATIR VRPDRTSVYA QYTVRALDRP AFEARLKDLG
VPTAVHYPAA LHKQPAYAAL AADAICPTAE QLAREVISLP MHPYLTQADQ DRIIDAATRA
SDPRVARA
//
