(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHW3_GEOS0

ID   A0A0F6BHW3_GEOS0        Unreviewed;       600 AA.
AC   A0A0F6BHW3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 23.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000256|SAAS:SAAS00887593};
DE            EC=2.6.1.16 {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=GFAT {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
GN   Name=glmS {ECO:0000256|HAMAP-Rule:MF_00164};
GN   OrderedLocusNames=GY4MC1_0158 {ECO:0000313|EMBL:ADP73014.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73014.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73014.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73014.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC         phosphate + L-glutamate; Xref=Rhea:RHEA:13237,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725,
CC         ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00164};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164,
CC       ECO:0000256|SAAS:SAAS00887591}.
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DR   EMBL; CP002293; ADP73014.1; -; Genomic_DNA.
DR   RefSeq; WP_003247646.1; NC_014650.1.
DR   EnsemblBacteria; ADP73014; ADP73014; GY4MC1_0158.
DR   GeneID; 29237194; -.
DR   KEGG; gmc:GY4MC1_0158; -.
DR   KO; K00820; -.
DR   OMA; ASEYRYA; -.
DR   OrthoDB; 43416at2; -.
DR   BioCyc; GSP581103:G1GOQ-197-MONOMER; -.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHW3.
DR   SWISS-2DPAGE; A0A0F6BHW3.
KW   Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:ADP73014.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000256|SAAS:SAAS00887588};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00164,
KW   ECO:0000313|EMBL:ADP73014.1}.
FT   INIT_MET      1      1       Removed. {ECO:0000256|HAMAP-Rule:
FT                                MF_00164}.
FT   DOMAIN        2    217       Glutamine amidotransferase type-2.
FT                                {ECO:0000259|PROSITE:PS51278}.
FT   DOMAIN      283    422       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   DOMAIN      452    590       SIS. {ECO:0000259|PROSITE:PS51464}.
FT   ACT_SITE      2      2       Nucleophile; for GATase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
FT   ACT_SITE    595    595       For Fru-6P isomerization activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_00164}.
SQ   SEQUENCE   600 AA;  65874 MW;  9E44E0E58E392489 CRC64;
     MCGIVGYIGQ HDVKEILLRG LEKLEYRGYD SAGIAMLNEE GIHLFKEKGR IADLRAVVDP
     NTSATLGIGH TRWATHGAPS RINAHPHQSA SGRFTLVHNG VIENYAILQQ EYLQDVALKS
     DTDTEIIVQL VEKFVNDGLS VEEAFRKTLT LLKGSYAIAM IDAENQEVIY VAKNKSPLLV
     GIGNGFNVVA SDAMAMLQVT NQFVELMDKE MVVVTRESMT IKNLNGDIIE RAPFTAELDA
     SDIEKGTYPH YMLKEIDEQP FVMRRIIQKY QDENGQLTIA PEVVAEVVNA DRLYIIACGT
     SYHAGLVGKQ LIEKWAKIPV EVHVASEFSY NMPLLSEKPL FIYISQSGET ADSRAVLVQT
     KKLGHKAITI TNVPGSTLSR EADYTLLLHA GPEIAVASTK AYTAQIAVLA ILATAAAKAK
     GIALDFDLKK ELGIIANVME MLCDAKEEME KIAREYLSTT RNCFFIGRAV DYYVCLEGAL
     KLKEISYIQA EGFAGGELKH GTIALIEDGT PVVALSTQEH VNLSIRGNVK EVVARGANPC
     IISMRGLETD EDRYVIPAVH PMLTPLVSVV PLQLIAYYAA LHRGCDVDKP RNLAKSVTVE
//

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