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Database: UniProt
Entry: A0A0S8KQE9_9BACE
LinkDB: A0A0S8KQE9_9BACE
Original site: A0A0S8KQE9_9BACE 
ID   A0A0S8KQE9_9BACE        Unreviewed;       406 AA.
AC   A0A0S8KQE9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Aminotransferase DegT {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMS23_06725 {ECO:0000313|EMBL:KPL23341.1};
OS   Bacteroides sp. SM1_62.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1703351 {ECO:0000313|EMBL:KPL23341.1, ECO:0000313|Proteomes:UP000054347};
RN   [1] {ECO:0000313|EMBL:KPL23341.1, ECO:0000313|Proteomes:UP000054347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM1_62 {ECO:0000313|EMBL:KPL23341.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPL23341.1}.
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DR   EMBL; LJVC01000138; KPL23341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8KQE9; -.
DR   PATRIC; fig|1703351.3.peg.643; -.
DR   Proteomes; UP000054347; 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:SF45; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN RFBH; 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        180
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         180
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   406 AA;  45525 MW;  9BF6F5CB986609DD CRC64;
     MQGWPCLDEK SIKAVEQVLR SGKVNYWTGP KGMEFERRFA AWQGSKFAIN VSSGTAALHV
     ALTALGIGPG DEVIVPSYTF IASPFSIIQA GAIPRFADVN IDDHCISVES SEKLINERTK
     AIMPVHLYGN VCEMDAINAL AKKHNLFVLE DNAEAFGGSY KGKKTGTLGD IAACSFCQNK
     TFTTGGEGGM VTTDNEELAW IAKSFRDHGY DVKQRLSLLE LEQKLPYIHN MVGWNYRMTE
     MQSAIGLAEL ERIDSWNMPS RRRNAHIIID RIKDLPQVLH VPIDTEERQN GWYVLAFSLD
     IDNMRCDIKD FVDAVGAEGA PVWKVFWPQC HTEKAFQEHR AFGRSGFPFT SREFSDVKSV
     DYSSVEVPNA VWHESHTFTC FAYPTYTPED CEQIGDALRK VILAYA
//
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