ID A0A0T9UCR2_YERAL Unreviewed; 266 AA. AC A0A0T9UCR2; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 22-FEB-2023, entry version 31. DE RecName: Full=Glucosamine-6-phosphate deaminase {ECO:0000256|HAMAP-Rule:MF_01241}; DE EC=3.5.99.6 {ECO:0000256|HAMAP-Rule:MF_01241}; DE AltName: Full=GlcN6P deaminase {ECO:0000256|HAMAP-Rule:MF_01241}; DE Short=GNPDA {ECO:0000256|HAMAP-Rule:MF_01241}; DE AltName: Full=Glucosamine-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01241}; GN Name=nagB {ECO:0000256|HAMAP-Rule:MF_01241, GN ECO:0000313|EMBL:CNL33143.1}; GN ORFNames=ERS137965_02733 {ECO:0000313|EMBL:CNL33143.1}; OS Yersinia aldovae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Yersiniaceae; Yersinia. OX NCBI_TaxID=29483 {ECO:0000313|EMBL:CNL33143.1, ECO:0000313|Proteomes:UP000041595}; RN [1] {ECO:0000313|EMBL:CNL33143.1, ECO:0000313|Proteomes:UP000041595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IP06005 {ECO:0000313|EMBL:CNL33143.1, RC ECO:0000313|Proteomes:UP000041595}; RA Murphy D.; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the reversible isomerization-deamination of CC glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) CC and ammonium ion. {ECO:0000256|HAMAP-Rule:MF_01241}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6- CC phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01241}; CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine 6- CC phosphate (GlcNAc6P). {ECO:0000256|HAMAP-Rule:MF_01241}. CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D- CC fructose 6-phosphate from N-acetylneuraminate: step 5/5. CC {ECO:0000256|HAMAP-Rule:MF_01241}. CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01241}. CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. NagB subfamily. {ECO:0000256|HAMAP-Rule:MF_01241}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01241}. 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; CQEJ01000015; CNL33143.1; -; Genomic_DNA. DR RefSeq; WP_004700761.1; NZ_CABHPY010000048.1. DR AlphaFoldDB; A0A0T9UCR2; -. DR STRING; 1453495.AT01_3766; -. DR EnsemblBacteria; CNL33143; CNL33143; ERS137965_02733. DR eggNOG; COG0363; Bacteria. DR OrthoDB; 9791139at2; -. DR UniPathway; UPA00629; UER00684. DR Proteomes; UP000041595; Unassembled WGS sequence. DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd01399; GlcN6P_deaminase; 1. DR Gene3D; 3.40.50.1360; -; 1. DR HAMAP; MF_01241; GlcN6P_deamin; 1. DR InterPro; IPR006148; Glc/Gal-6P_isomerase. DR InterPro; IPR004547; Glucosamine6P_isomerase. DR InterPro; IPR018321; Glucosamine6P_isomerase_CS. DR InterPro; IPR037171; NagB/RpiA_transferase-like. DR PANTHER; PTHR11280; GLUCOSAMINE-6-PHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR11280:SF5; GLUCOSAMINE-6-PHOSPHATE ISOMERASE; 1. DR Pfam; PF01182; Glucosamine_iso; 1. DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1. DR TIGRFAMs; TIGR00502; nagB; 1. DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1. PE 3: Inferred from homology; KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_01241}; KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01241}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01241, ECO:0000313|EMBL:CNL33143.1}. FT DOMAIN 10..230 FT /note="Glucosamine/galactosamine-6-phosphate isomerase" FT /evidence="ECO:0000259|Pfam:PF01182" FT ACT_SITE 72 FT /note="Proton acceptor; for enolization step" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" FT ACT_SITE 141 FT /note="For ring-opening step" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" FT ACT_SITE 143 FT /note="Proton acceptor; for ring-opening step" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" FT ACT_SITE 148 FT /note="For ring-opening step" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" FT SITE 151 FT /note="Part of the allosteric site" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" FT SITE 158 FT /note="Part of the allosteric site" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" FT SITE 160 FT /note="Part of the allosteric site" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" FT SITE 161 FT /note="Part of the allosteric site" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" SQ SEQUENCE 266 AA; 29554 MW; CFC1FDE4C4FBD91B CRC64; MRLIPLKNTT EVGKWAARHI VNRINAFKPT AERPFVLGLP TGGTPMEAYK HLVALHKAGE VSFKNVVTFN MDEYVGLPKE HPESYYTFMH SNFFNHVDIP AENINLLNGN AADIDAECRR YEEKIKSYGK IHLFMGGVGV DGHIAFNEPA SSLASRTRIK TLTQETRIAN SRFFGGDANL VPKYALTVGV GTLLDAEEVM ILVTGHGKAQ ALQAAVEGSI NHMWTISCLQ LHAKAIMVCD EPSTMELKVK TVKYFHELEA ENIKDL //