ID   A0A0S7XHC5_9BACT        Unreviewed;       407 AA.
AC   A0A0S7XHC5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   08-NOV-2023, entry version 25.
DE   RecName: Full=Glutamine--scyllo-inositol aminotransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMS15_05620 {ECO:0000313|EMBL:KPJ61863.1};
OS   Planctomycetes bacterium DG_23.
OC   Bacteria; Planctomycetota.
OX   NCBI_TaxID=1703414 {ECO:0000313|EMBL:KPJ61863.1, ECO:0000313|Proteomes:UP000052166};
RN   [1] {ECO:0000313|EMBL:KPJ61863.1, ECO:0000313|Proteomes:UP000052166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG_23 {ECO:0000313|EMBL:KPJ61863.1};
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:KPJ61863.1}.
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DR   EMBL; LIZR01000064; KPJ61863.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S7XHC5; -.
DR   STRING; 1703414.AMS15_05620; -.
DR   Proteomes; UP000052166; 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   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         195
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   407 AA;  44332 MW;  5E387F9AA20247AA CRC64;
     MTLAAKGGRP VRTEPFPKRT PFGEEELKLV TQALQSQNLF SVRGTMVKGL EEEFAAAYGM
     KKAIASSSGT ASLHIAIGAL DLEPGDEVIL GPITDAGSLI GILYQNAIPI FADIDPQTFN
     LDPADVQRKI TERTRAIMAI YLFGNASGAL EVAEVAKKGG IPLVEDASQA HMTRCRGRLL
     GTLGEIGCFS LQQSKHMTSG DGGVSITNNE ALAQRMALFR DKGWDRTTTG TGPRDYLFLA
     PNYRMTELQG AVALAQLKKV RSVVERRFHL GRYLSDLISE IPGVRTQKVE EGSEHSYWSF
     ALISEKIPVA DFAQALKAEG IPAGTGYIGE PIYIRHRALK EKKTYGTSGC PFTCKFASRK
     YEYRKGDCPN AERVLSQMVT LSINENYGDK DIEDMAAGVN KVARALS
//