ID E8WV47_GEOS8 Unreviewed; 369 AA.
AC E8WV47;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Glutamine--scyllo-inositol transaminase {ECO:0000313|EMBL:ADW15586.1};
DE EC=2.6.1.50 {ECO:0000313|EMBL:ADW15586.1};
GN OrderedLocusNames=GM18_4172 {ECO:0000313|EMBL:ADW15586.1};
OS Geobacter sp. (strain M18).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW15586.1, ECO:0000313|Proteomes:UP000001442};
RN [1] {ECO:0000313|EMBL:ADW15586.1, ECO:0000313|Proteomes:UP000001442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M18 {ECO:0000313|EMBL:ADW15586.1,
RC ECO:0000313|Proteomes:UP000001442};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D.,
RA Aklujkar M., Lovley D., Woyke T.;
RT "Complete sequence of Geobacter sp. M18.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP002479; ADW15586.1; -; Genomic_DNA.
DR AlphaFoldDB; E8WV47; -.
DR STRING; 443143.GM18_4172; -.
DR KEGG; geb:GM18_4172; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_6_0_7; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000001442; Chromosome.
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: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:ADW15586.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:ADW15586.1}.
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 369 AA; 39062 MW; 4214A7B2C02DC042 CRC64;
MADTVAVANP QAQFLAHEAG IRAAIDRVLA GGWYILGSEV RGFEEEFASF VGVPHAVGVA
SGTDALALAL LSVGVRPGDE VITVSHSAVA TAAAVEQIGA VPVFADIDPA TRCLDPERLP
ALLSPRTRAL LPVHVYGQPA PMGRIMEAAR RHGLKVVEDC AQAHGAEIDG RRVGSFGDAA
AFSFYPTKNL GAIGDGGAVV TGSPEVAADL RARREYGWQE RYISAFAGLN SRLDELQAAI
LRVKLPHLAA DNARRREIAA RYDAALSGSG VVAPARIPGT LHAMHLYVVE CAGRERLQEH
LKTAGIATAR HYPAPIHLQP AYRGRIRGGD LLPVTETLYG RIVSLPMYPE LTDGEVRRVA
GALAAYAPC
//
