ID A0A1I1YSW5_9FLAO Unreviewed; 641 AA.
AC A0A1I1YSW5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=SAMN04488131_101118 {ECO:0000313|EMBL:SFE22551.1};
OS Flavobacterium xueshanense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=935223 {ECO:0000313|EMBL:SFE22551.1, ECO:0000313|Proteomes:UP000198596};
RN [1] {ECO:0000313|EMBL:SFE22551.1, ECO:0000313|Proteomes:UP000198596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9227 {ECO:0000313|EMBL:SFE22551.1,
RC ECO:0000313|Proteomes:UP000198596};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- 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 -!- 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; FONQ01000001; SFE22551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1YSW5; -.
DR STRING; 935223.SAMN04488131_101118; -.
DR OrthoDB; 9791139at2; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000198596; 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 Gene3D; 3.40.50.10320; LmbE-like; 1.
DR HAMAP; MF_01241; GlcN6P_deamin; 1.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR004547; Glucosamine6P_isomerase.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR NCBIfam; TIGR00502; nagB; 1.
DR PANTHER; PTHR42892:SF1; GLUCOSAMINE-6-PHOSPHATE DEAMINASE; 1.
DR PANTHER; PTHR42892; GLUCOSAMINE-6-PHOSPHATE DEAMINASE-LIKE PROTEIN BT_0258-RELATED; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; LmbE-like; 1.
DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01241};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01241}.
FT DOMAIN 32..258
FT /note="Glucosamine/galactosamine-6-phosphate isomerase"
FT /evidence="ECO:0000259|Pfam:PF01182"
FT ACT_SITE 93
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
FT ACT_SITE 166
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
FT ACT_SITE 171
FT /note="For ring-opening step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
SQ SEQUENCE 641 AA; 73173 MW; 1682B6D7C6EBA19A CRC64;
MKTKTSLAYN IPGKFEETRF EKNHNVIFKS AVEASKVVAQ EIAVLIKSKQ VENKFCILGL
ATGSSPIKVY EELVRMHKED GLSFHNVVTF NLDEYYPMTK ENRQSYHYFM HQHLFNHVDI
KPENINIPDG TVVLEELNQY CMNYETKIKN AGGIDFQLLG IGRTGHVGFN EPGSHINSGT
RIITLDHITR VDASSDFNGI DNVPKRAITM GVSTILRSKR IVLMAWGQNK ATVIKRTIQG
EITSEVPATF LQNHSNATFV LDQFAASELT RFETPWLVGQ CIWTQELKSK AIIWLCKETK
QSILKLTDRD YNNNGMSDLL AQEGSAYDLN INMFNVLQHT ITGWPGGKPN TDDSHRPERA
NPSKKRVILF SPHPDDDVIS MGGTFSKLIK QGHDVHVVYQ TSGNIAVTDD EALKFAEVCR
DFIGKENSEI NFSSVINFLN NKTENQVDSL EVRKLKGLIR RRESYAATRY IGLKDEKTHF
LDLPFYETGQ IKKNPVGLDD IAIVKDIIAK IKPHQVFAAG DLADPHGTHE VCLNSIFEAM
KQLKSESYMN DCWLWLYRGA WHEWDIHEID MAVPLSPDEV TIKRHAILYH QSQKDRVMFQ
GNDSREFWVR AEERNKNTAK LYDDLGLAEY EAIEAFKRYD Y
//
