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Database: UniProt
Entry: A0A3N2NA40_9BACT
LinkDB: A0A3N2NA40_9BACT
Original site: A0A3N2NA40_9BACT 
ID   A0A3N2NA40_9BACT        Unreviewed;       377 AA.
AC   A0A3N2NA40;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 11.
DE   SubName: Full=DegT/DnrJ/EryC1/StrS family aminotransferase {ECO:0000313|EMBL:ROT18564.1};
GN   ORFNames=EEL51_09700 {ECO:0000313|EMBL:ROT18564.1};
OS   Muribaculaceae bacterium Isolate-110 (HZI).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX   NCBI_TaxID=2486473 {ECO:0000313|EMBL:ROT18564.1, ECO:0000313|Proteomes:UP000275373};
RN   [1] {ECO:0000313|EMBL:ROT18564.1, ECO:0000313|Proteomes:UP000275373}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate-110 (HZI) {ECO:0000313|Proteomes:UP000275373};
RA   Clavel T., Strowig T.;
RT   "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT   host preference, and functional potential of this yet undescribed family.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:ROT18564.1}.
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DR   EMBL; RIBL01000016; ROT18564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2NA40; -.
DR   OrthoDB; 9810913at2; -.
DR   Proteomes; UP000275373; 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:ROT18564.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275373};
KW   Transferase {ECO:0000313|EMBL:ROT18564.1}.
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         196
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   377 AA;  40546 MW;  E4A36C5F33A812ED CRC64;
     MKYPFLDLGE VNRPYMDEMT EAAIRVIRSG RYIGGEEVES LESRLAAMTG SCHAIGVSNG
     LDALRLILRA YVVLGAMSEG DEVIVPANTY IASVLAISDA GLKPVLVDVD DSTMNIDTSL
     IENAITERTK AIMTVHLYGR VAWDNTLVDI ARNHGLKIIE DCAQAIGARA VTAGLGGGVH
     AGALGDAGAF SFYPTKNVGA LGDAGAVTTD DTLLASTIRA LANYGSDRRY HNIYQGYNCR
     MDPIQAAMLN VKLTHTDDEN ADRFARALAY SRTISHPDVV TPLMSKAVID NVWHQYVIRV
     RDGKRDRMRQ LLAEAGVGTD IHYATPPHMQ PCYAGLGHAS LPVTELLADE IISLPIGTGT
     SVKDAAEIGE IINHITL
//
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