ID A0A0T9UCR2_YERAL Unreviewed; 266 AA. AC A0A0T9UCR2; DT 17-FEB-2016, integrated into UniProtKB/TrEMBL. DT 17-FEB-2016, sequence version 1. DT 12-SEP-2018, entry version 18. 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 CC (Fru6P) and ammonium ion. {ECO:0000256|HAMAP-Rule:MF_01241}. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 6-phosphate + H(2)O = D- CC fructose 6-phosphate + NH(3). {ECO:0000256|HAMAP-Rule:MF_01241, CC ECO:0000256|SAAS:SAAS00900181}. CC -!- ACTIVITY REGULATION: Allosterically activated by N- CC acetylglucosamine 6-phosphate (GlcNAc6P). {ECO:0000256|HAMAP- CC Rule:MF_01241}. CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; CC D-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- CC Rule:MF_01241}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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_CQEJ01000015.1. DR EnsemblBacteria; CNL33143; CNL33143; ERS137965_02733. 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 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; PTHR11280; 1. DR Pfam; PF01182; Glucosamine_iso; 1. DR SUPFAM; SSF100950; SSF100950; 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 ECO:0000256|SAAS:SAAS00900172}; Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000041595}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01241, KW ECO:0000256|SAAS:SAAS00900180, ECO:0000313|EMBL:CNL33143.1}. FT DOMAIN 9 230 Glucosamine_iso. {ECO:0000259|Pfam: FT PF01182}. FT COILED 104 124 {ECO:0000256|SAM:Coils}. FT ACT_SITE 72 72 Proton acceptor; for enolization step. FT {ECO:0000256|HAMAP-Rule:MF_01241}. FT ACT_SITE 141 141 For ring-opening step. FT {ECO:0000256|HAMAP-Rule:MF_01241}. FT ACT_SITE 143 143 Proton acceptor; for ring-opening step. FT {ECO:0000256|HAMAP-Rule:MF_01241}. FT ACT_SITE 148 148 For ring-opening step. FT {ECO:0000256|HAMAP-Rule:MF_01241}. FT SITE 151 151 Part of the allosteric site. FT {ECO:0000256|HAMAP-Rule:MF_01241}. FT SITE 158 158 Part of the allosteric site. FT {ECO:0000256|HAMAP-Rule:MF_01241}. FT SITE 160 160 Part of the allosteric site. FT {ECO:0000256|HAMAP-Rule:MF_01241}. FT SITE 161 161 Part of the allosteric site. FT {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 //