ID D9PZM7_ACIS3 Unreviewed; 614 AA. AC D9PZM7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 14-OCT-2015, entry version 37. DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|HAMAP-Rule:MF_00164}; DE EC=2.6.1.16 {ECO:0000256|HAMAP-Rule:MF_00164, ECO:0000313|EMBL:ADL18515.1}; 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=ASAC_0107 {ECO:0000313|EMBL:ADL18515.1}; OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 / OS 345-15). OC Archaea; Crenarchaeota; Thermoprotei; Acidilobales; Acidilobaceae; OC Acidilobus. OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18515.1, ECO:0000313|Proteomes:UP000000346}; RN [1] {ECO:0000313|EMBL:ADL18515.1, ECO:0000313|Proteomes:UP000000346} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15 RC {ECO:0000313|Proteomes:UP000000346}; 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. {ECO:0000256|HAMAP-Rule:MF_00164}. CC -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L- CC glutamate + D-glucosamine 6-phosphate. {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 -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000256|HAMAP-Rule:MF_00164}. CC -!- SIMILARITY: Contains 2 SIS domains. {ECO:0000256|HAMAP- CC Rule:MF_00164}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001742; ADL18515.1; -; Genomic_DNA. DR RefSeq; WP_013266027.1; NC_014374.1. DR RefSeq; YP_003815546.1; NC_014374.1. DR ProteinModelPortal; D9PZM7; -. DR STRING; 666510.ASAC_0107; -. DR MEROPS; C44.971; -. DR EnsemblBacteria; ADL18515; ADL18515; ASAC_0107. DR GeneID; 9498320; -. DR KEGG; asc:ASAC_0107; -. DR HOGENOM; HOG000258896; -. DR KO; K00820; -. DR OMA; GEFFCAS; -. DR BioCyc; ASAC666510:GH9G-109-MONOMER; -. DR Proteomes; UP000000346; Chromosome. 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:UniProtKB-HAMAP. DR GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_00164; GlmS; 1. DR InterPro; IPR017932; GATase_2_dom. 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; KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164, KW ECO:0000313|EMBL:ADL18515.1}; KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_00164}; KW Complete proteome {ECO:0000313|Proteomes:UP000000346}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164}; KW Reference proteome {ECO:0000313|Proteomes:UP000000346}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_00164}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00164, KW ECO:0000313|EMBL:ADL18515.1}. FT INIT_MET 1 1 Removed. {ECO:0000256|HAMAP-Rule: FT MF_00164}. FT DOMAIN 2 220 Glutamine amidotransferase type-2. FT {ECO:0000256|HAMAP-Rule:MF_00164}. FT DOMAIN 290 429 SIS 1. {ECO:0000256|HAMAP-Rule:MF_00164}. FT DOMAIN 459 604 SIS 2. {ECO:0000256|HAMAP-Rule:MF_00164}. FT ACT_SITE 2 2 Nucleophile; for GATase activity. FT {ECO:0000256|HAMAP-Rule:MF_00164}. FT ACT_SITE 609 609 For Fru-6P isomerization activity. FT {ECO:0000256|HAMAP-Rule:MF_00164}. 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 //