ID A0A3L9ZRF4_9FLAO Unreviewed; 640 AA.
AC A0A3L9ZRF4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=BC961_2591 {ECO:0000313|EMBL:RMA72995.1};
OS Flavobacterium weaverense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=271156 {ECO:0000313|EMBL:RMA72995.1, ECO:0000313|Proteomes:UP000280368};
RN [1] {ECO:0000313|EMBL:RMA72995.1, ECO:0000313|Proteomes:UP000280368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19727 {ECO:0000313|EMBL:RMA72995.1,
RC ECO:0000313|Proteomes:UP000280368};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RMA72995.1}.
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DR EMBL; REFH01000011; RMA72995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L9ZRF4; -.
DR OrthoDB; 9791139at2; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000280368; 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 31..258
FT /note="Glucosamine/galactosamine-6-phosphate isomerase"
FT /evidence="ECO:0000259|Pfam:PF01182"
FT REGION 345..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 640 AA; 73002 MW; 4F6FEB487875C2D2 CRC64;
MKNSAPLQYD IPGKFEETRF EKNHNVIFKS ASDASKYVAE EIAQLIRFKQ SRYESCVLGL
ATGSSPIKVY EELVRMHQED GLSFHNVITF NLDEYYPMTK ENRQSYHYFM QEHLFNHVDI
RPENINIPDG TILLSQVNQY CIDYDNKIKQ AGGIDLQLLG IGRTGHVGFN EPGSHINSGT
RIITLDHITR IDASSAFNGT ANVPKRAITM GVSTILRSKR ILLLAWGQNK AEIIKRTIQG
EITSEVPATF LQNHNNTTFV LDQFAASELT RFKTPWLVGE CIWTQELKSK AIIWLCKETK
QSILKLTDRD YNNNGMSDLL AQEGSAYDLN INMFNVLQHT ITGWPGGKPN TDDSNRPERS
NPSKKRIILF SPHPDDDVIS MGGTFSKLIK QGHDVHVVYQ TSGNIAVTDD EALKFAEVCN
DFISNENSTT FSSVISDLNT KSENEVDSLE VRKLKGLIRR RESYAATRYI GLKDENTHFL
DLPFYETGQI KKNPLAKEDI DIVAAIISKI KPHQVFAAGD LADPHGTHEV CLNAIFAAMK
ELKKESFMDD CWLWLYRGAW HEWDLHEIDM AVPLSPDEVL MKRHAILYHQ SQKDRVMFQG
NDSREFWVRA EDRNKNTAKL YDDLGLAQYE AIEAFKRFDY
//
