ID A0A1U7GQ70_9BACT Unreviewed; 392 AA.
AC A0A1U7GQ70;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:OJW24572.1};
GN ORFNames=BGO49_05890 {ECO:0000313|EMBL:OJW24572.1};
OS Planctomycetales bacterium 71-10.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX NCBI_TaxID=1895807 {ECO:0000313|EMBL:OJW24572.1, ECO:0000313|Proteomes:UP000185848};
RN [1] {ECO:0000313|EMBL:OJW24572.1, ECO:0000313|Proteomes:UP000185848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=71-10 {ECO:0000313|EMBL:OJW24572.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJW24572.1}.
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DR EMBL; MKTT01000036; OJW24572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7GQ70; -.
DR STRING; 1895807.BGO49_05890; -.
DR Proteomes; UP000185848; 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: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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}.
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 193
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 392 AA; 43311 MW; 928939569E8B1ED5 CRC64;
MAVPYEPAGV PALNLRAQYR TIRDEIEPVV REVMETQGFV MGPEVANLES EIAEYCGAAH
AVGCASGTDA LLLPLMAIDL GPGDEVITTP YTFFATGGSI WRTGARPVFV DIEPDTFNID
PGAIEAAITE RTKAIIPVHL YGQAADMDPI REIAARRDLM VLEDAAQAIG AAYNGRRTGT
LGTVAAFSFY PSKNLGGFGD GGMVATDDPV LARRIARLRV HGMEPKYHHH EVGLNSRLDA
LQAAVLRVKL RHLDEWTVAR REAADRYRDL FASHGMDEMV RLPVERPGNY HVYNQYVVRV
PASIRDDMRQ HLAERKIGTE IYYPIPLHLQ PCFASLGCKP GDFPRTEAAA RETIALPIYP
ELTEAEQRYV VGAMHQFLHE RAHPSLFTDR AA
//
