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Database: UniProt
Entry: A0A1F6AX38_9BACT
LinkDB: A0A1F6AX38_9BACT
Original site: A0A1F6AX38_9BACT 
ID   A0A1F6AX38_9BACT        Unreviewed;       371 AA.
AC   A0A1F6AX38;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Aminotransferase DegT {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2973_00640 {ECO:0000313|EMBL:OGG29093.1};
OS   Candidatus Gottesmanbacteria bacterium RIFCSPLOWO2_01_FULL_49_10.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1798396 {ECO:0000313|EMBL:OGG29093.1, ECO:0000313|Proteomes:UP000176409};
RN   [1] {ECO:0000313|EMBL:OGG29093.1, ECO:0000313|Proteomes:UP000176409}
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:OGG29093.1}.
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DR   EMBL; MFJZ01000058; OGG29093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6AX38; -.
DR   STRING; 1798396.A2973_00640; -.
DR   Proteomes; UP000176409; 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:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2}.
FT   ACT_SITE        187
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         187
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   371 AA;  41953 MW;  906D8CB1A3046B99 CRC64;
     MWQPSKMILT AGPKIGKNDI RYVSDAVKNG WNLHHSDYIY KFEEAFAKYV NAKYTLSMPH
     GTSALHIALV CMGVGRGDEV IVPDLTYVTC ANVVHQLGAI PILVDIDRET WSIDTSRLEK
     YITKKTKVIM PVHLYGNIAD MDGIAQIAKK HHLHILEDAC EGLGSTLHGK QVGSLSDAAA
     FSFQGAKLLS IGEGGMLVTK HKGWIERARS IVDNGISFTR QFWHNEIGYM YAMSNIQAAL
     GLSRLEDIDD LIARKRRINR WYRERLGGIK GIQFSPERKG VVSSFWMNTI VLDTDFGITR
     DELRIKMSEM KIDTRPFFFP ISEFCFYNKQ PINNPVSYHV SHNGINLPSG VMLTERMVDY
     IASVIRKLLL K
//
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