ID A0A1F7IE04_9BACT Unreviewed; 360 AA.
AC A0A1F7IE04;
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=Aminotransferase DegT {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2954_06915 {ECO:0000313|EMBL:OGK41587.1};
OS Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_37_12.
OC Bacteria; Candidatus Roizmanbacteria.
OX NCBI_TaxID=1802056 {ECO:0000313|EMBL:OGK41587.1, ECO:0000313|Proteomes:UP000177698};
RN [1] {ECO:0000313|EMBL:OGK41587.1, ECO:0000313|Proteomes:UP000177698}
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:OGK41587.1}.
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DR EMBL; MGAG01000010; OGK41587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7IE04; -.
DR STRING; 1802056.A2954_06915; -.
DR Proteomes; UP000177698; Unassembled WGS sequence.
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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 175
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 360 AA; 40534 MW; 542428755E4E49E0 CRC64;
MTKEKIMKVS LTKPSIDSKE LKAVERVLKS GWLIRGKETK AFEEEFAAYS GAKYGVATNG
CTMALYLAVK QLKLKAGDEV IVPSLTWSAT ASIVIQAGLT PVFADVKKSD WCLDPKDVKS
KITKKTKLVI PVHYSGKFAI GFENISIPVI YDSAHRIEKK DFTGVTSCYS FYAVKNMMTV
RGGMILTNDE KAAKYYAMLC HGGLDKDTFS RYLGGKTQHD ASSFYYEIVE PGWNFDMTDL
EAAIGREQLK KIDVLNKKRM KVVEKYNKAF GLKNTGDHFY PILVENRDEF LVSMKEVGIQ
CGIHYLPLHL MKGYKEYRTS LPVTEYIGKR CVTLPLHPEL ASEEVEFVIQ KTKDTAQFSA
//
