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Database: UniProt
Entry: A8M6D5_SALAI
LinkDB: A8M6D5_SALAI
Original site: A8M6D5_SALAI 
ID   A8M6D5_SALAI            Unreviewed;       388 AA.
AC   A8M6D5;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:ABV97160.1};
DE            EC=2.6.1.50 {ECO:0000313|EMBL:ABV97160.1};
GN   OrderedLocusNames=Sare_1255 {ECO:0000313|EMBL:ABV97160.1};
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=391037 {ECO:0000313|EMBL:ABV97160.1};
RN   [1] {ECO:0000313|EMBL:ABV97160.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205 {ECO:0000313|EMBL:ABV97160.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA   Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU004508}.
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DR   EMBL; CP000850; ABV97160.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8M6D5; -.
DR   STRING; 391037.Sare_1255; -.
DR   KEGG; saq:Sare_1255; -.
DR   PATRIC; fig|391037.6.peg.1273; -.
DR   eggNOG; COG0399; Bacteria.
DR   HOGENOM; CLU_033332_7_1_11; -.
DR   OMA; YMAMFRV; -.
DR   OrthoDB; 9804264at2; -.
DR   GO; GO:0047310; F:glutamine-scyllo-inositol transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080100; F:L-glutamine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
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   Aminotransferase {ECO:0000313|EMBL:ABV97160.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:ABV97160.1}.
FT   ACT_SITE        188
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         188
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   388 AA;  42371 MW;  F6DED36BEF9A0B7C CRC64;
     MDARQAPEFP AWPQYDDAER AGLIRALEQG QWWRMGGDEV NSFEHEFADH HGAEHALAVT
     NGTHALELAL QVLGVGPGTE VIVPAFTFIS SSQAVQRLGA VTVPVDVDPH TYNIDPAAVA
     AAVTPRTKVI MPVHMAGLMA DMDALAKISA DNGVPLLQDA AHAHGARWRG NRVGELGSIA
     TFSFQNGKLM TAGEGGAVVF PEGEAERYET AFLRHSCGRP RDDRRYLHRV SGSNMRLNEF
     SASVLRAQLR RLDQQIAVRD QRWTLLSQLL GAIDGVVPQG GDERADRNSH YMAMFRVPGI
     GEKERNALVD RLVAMGLPAF AGFRAIYRTD AFWELGTPDE SLDAIAERCP HTDAISEDCV
     WLHHRILLAG EQEMRATAEL VSDAVASA
//
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