ID   L9WZ34_9EURY            Unreviewed;       448 AA.
AC   L9WZ34;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:ELY54667.1};
GN   ORFNames=C491_18734 {ECO:0000313|EMBL:ELY54667.1};
OS   Natronococcus amylolyticus DSM 10524.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=1227497 {ECO:0000313|EMBL:ELY54667.1, ECO:0000313|Proteomes:UP000011688};
RN   [1] {ECO:0000313|EMBL:ELY54667.1, ECO:0000313|Proteomes:UP000011688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10524 {ECO:0000313|EMBL:ELY54667.1,
RC   ECO:0000313|Proteomes:UP000011688};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY54667.1}.
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DR   EMBL; AOIB01000036; ELY54667.1; -; Genomic_DNA.
DR   AlphaFoldDB; L9WZ34; -.
DR   STRING; 1227497.C491_18734; -.
DR   PATRIC; fig|1227497.3.peg.3824; -.
DR   eggNOG; arCOG00118; Archaea.
DR   Proteomes; UP000011688; 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|RuleBase:RU004508}.
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  47474 MW;  0A507B1826FC59D6 CRC64;
     MGDGSVRTTK NGRSARASNS SGSRPSSTET TPFDRVVNGY LPFGFPNRFA MSDDIPLFEI
     AWDERDVQNA VDSITRGSYW ANGPYVEAFE DGLERYLGVE HAVTVNSGTT ALVAALEAHG
     VGEGDEVVVP AFTFIATANA VRLVGAEPTF ADIEPDTYGL DPGAVADAIT ERTAAIVPVH
     PYGAPCRIAE IAAVAAEADV PVIEDAAEAF GSSSRGRAVG TFGETAALSF CQNKILPTGE
     GGAVVTDDDD LARRLERFRS HGRASAEYFD SAASGDYVGL GTNIRMSDLV AAVGCAQLEK
     VDELIAERRR VAERYATGLA GIDGIEPQPE PADGRHVRQL YTVTLAPGAD REAVIETLSE
     RGIASKIYWD PPVHLTDAYR DRHERGSLPV TEAVSGCVLS LPMSPVFDND AVDRVVDGLK
     AALESPRVAG VADRRGSRTA DDGLESGR
//