ID   D9PZM7_ACIS3            Unreviewed;       614 AA.
AC   D9PZM7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   28-NOV-2012, entry version 19.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE            EC=2.6.1.16;
DE   AltName: Full=D-fructose-6-phosphate amidotransferase;
DE   AltName: Full=GFAT;
DE   AltName: Full=Glucosamine-6-phosphate synthase;
DE   AltName: Full=Hexosephosphate aminotransferase;
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase;
GN   Name=glmS; OrderedLocusNames=ASAC_0107;
OS   Acidilobus saccharovorans (strain DSM 16705 / VKM B-2471 / 345-15).
OC   Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus.
OX   NCBI_TaxID=666510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16705 / VKM B-2471 / 345-15;
RX   PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA   Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "The genome sequence of the crenarchaeon Acidilobus saccharovorans
RT   supports a new order, Acidilobales, and suggests an important
RT   ecological role in terrestrial acidic hot springs.";
RL   Appl. Environ. Microbiol. 76:5652-5657(2010).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L-
CC       glutamate + D-glucosamine 6-phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
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DR   EMBL; CP001742; ADL18515.1; -; Genomic_DNA.
DR   RefSeq; YP_003815546.1; NC_014374.1.
DR   ProteinModelPortal; D9PZM7; -.
DR   GeneID; 9498320; -.
DR   GenomeReviews; CP001742_GR; ASAC_0107.
DR   KEGG; asc:ASAC_0107; -.
DR   HOGENOM; HOG000258896; -.
DR   KO; K00820; -.
DR   OMA; RGNDPDK; -.
DR   BioCyc; ASAC666510:GH9G-109-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:HAMAP.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:HAMAP.
DR   HAMAP; MF_00164; GlmS; 1; -.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR001347; SIS.
DR   Pfam; PF01380; SIS; 2.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   DOMAIN        2    220       Glutamine amidotransferase type-2 (By
FT                                similarity).
FT   ACT_SITE      2      2       Nucleophile; for GATase activity (By
FT                                similarity).
FT   ACT_SITE    609    609       For Fru-6P isomerization activity (By
FT                                similarity).
SQ   SEQUENCE   614 AA;  66007 MW;  0F603380D9A93082 CRC64;
     MCGIIGATAN CSDVVPLIIR GLQRLEYRGY DSVGIAVVGN NELAVRKGAG ELEVVRRRLS
     LDEMRGLTGI GHTRWATHGP PNDVNAHPHT DCTGTIAIVH NGVIRNYASL KEELLARGHR
     IRSDTDTELV AHLIEEGVKE GKDFVSALAQ ALSRVEGTYA FAIVNSREPD RVYFAKNRSP
     LLVGVGDKVK AVASDVPALL DITRDIVFLE DGEFGYVTPR EVVIYRLTPS GYERLSDEEV
     RSRVRHVDIS PEAASKGGYP HFMIKEIYEQ PQAVRDTYEG NVEDPALGRV SSAILSANKV
     IVVAAGTSYH AGLVFSSLLA RRAGILAHTI ISSELPYLVD SIDGGDLVIA VSQSGETYDT
     LEAVRKAKER GAAVVGVTNV LGSALDRESQ LRLYTRAGPE IGVAATKTFL SQVMLLELLS
     IRAGEASGRL RPSEANELLR ALREVPQVLA NTLEASDPVA TALSKGLSGS AYILGRGLGA
     AIAREGALKV KEIAYVHAEA YPAGESKHGP IALVERGFPV FIVATSDARE VAGNAVEMAA
     RGARVYVVKP ADLGLELEGR ESITRIDMPP SSGVLELEPF ILTPLFQLLS YRVAVSRGYN
     PDKPRNLAKT VTVE
//