ID D9PZM7_ACIS3 Unreviewed; 614 AA. AC D9PZM7; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-NOV-2024, entry version 78. 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}; 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; Thermoproteota; 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 supports RT a new order, Acidilobales, and suggests an important ecological role in RT terrestrial acidic hot springs."; RL Appl. Environ. Microbiol. 76:5652-5657(2010). CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source. CC {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, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; CC Evidence={ECO:0000256|ARBA:ARBA00001031, 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 --------------------------------------------------------------------------- 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 AlphaFoldDB; D9PZM7; -. DR STRING; 666510.ASAC_0107; -. DR GeneID; 9498320; -. DR KEGG; asc:ASAC_0107; -. DR eggNOG; arCOG00057; Archaea. DR HOGENOM; CLU_012520_7_0_2; -. DR InParanoid; D9PZM7; -. DR OrthoDB; 372195at2157; -. DR Proteomes; UP000000346; 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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:TreeGrafter. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:TreeGrafter. DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:TreeGrafter. DR CDD; cd00714; GFAT; 1. DR CDD; cd05008; SIS_GlmS_GlmD_1; 1. DR CDD; cd05009; SIS_GlmS_GlmD_2; 1. DR FunFam; 3.40.50.10490:FF:000001; Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; 1. DR FunFam; 3.60.20.10:FF:000006; Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR HAMAP; MF_00164; GlmS; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR005855; GFAT. DR InterPro; IPR047084; GFAT_N. DR InterPro; IPR035466; GlmS/AgaS_SIS. DR InterPro; IPR035490; GlmS/FrlB_SIS. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR001347; SIS_dom. DR InterPro; IPR046348; SIS_dom_sf. DR NCBIfam; TIGR01135; glmS; 1. DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1. DR PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1. DR Pfam; PF13522; GATase_6; 1. DR Pfam; PF01380; SIS; 2. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR SUPFAM; SSF53697; SIS domain; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. DR PROSITE; PS51464; SIS; 2. PE 3: Inferred from homology; KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP- KW Rule:MF_00164}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164}; KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962}; KW Reference proteome {ECO:0000313|Proteomes:UP000000346}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00164}. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164" FT DOMAIN 2..220 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000259|PROSITE:PS51278" FT DOMAIN 290..429 FT /note="SIS" FT /evidence="ECO:0000259|PROSITE:PS51464" FT DOMAIN 459..604 FT /note="SIS" FT /evidence="ECO:0000259|PROSITE:PS51464" FT ACT_SITE 2 FT /note="Nucleophile; for GATase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164" FT ACT_SITE 609 FT /note="For Fru-6P isomerization activity" FT /evidence="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 //