ID F9YVR7_CAPCC Unreviewed; 647 AA.
AC F9YVR7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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 OrderedLocusNames=Ccan_11150 {ECO:0000313|EMBL:AEK23231.1};
OS Capnocytophaga canimorsus (strain 5).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK23231.1, ECO:0000313|Proteomes:UP000008895};
RN [1] {ECO:0000313|EMBL:AEK23231.1, ECO:0000313|Proteomes:UP000008895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX PubMed=21914877; DOI=10.1128/JB.05853-11;
RA Manfredi P., Pagni M., Cornelis G.R.;
RT "Complete genome sequence of the dog commensal and human pathogen
RT Capnocytophaga canimorsus strain 5.";
RL J. Bacteriol. 193:5558-5559(2011).
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}.
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DR EMBL; CP002113; AEK23231.1; -; Genomic_DNA.
DR RefSeq; WP_013997221.1; NC_015846.1.
DR AlphaFoldDB; F9YVR7; -.
DR STRING; 860228.Ccan_11150; -.
DR KEGG; ccm:Ccan_11150; -.
DR eggNOG; COG0363; Bacteria.
DR eggNOG; COG2120; Bacteria.
DR HOGENOM; CLU_425041_0_0_10; -.
DR OrthoDB; 9791139at2; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000008895; Chromosome.
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, ECO:0000313|EMBL:AEK23231.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008895}.
FT DOMAIN 35..261
FT /note="Glucosamine/galactosamine-6-phosphate isomerase"
FT /evidence="ECO:0000259|Pfam:PF01182"
FT ACT_SITE 98
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
FT ACT_SITE 171
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
FT ACT_SITE 176
FT /note="For ring-opening step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
SQ SEQUENCE 647 AA; 74015 MW; 79E1C11F723B5D83 CRC64;
MSNIDKNKLQ SIDYQRAGLF EETRYEKIHN VIFSDSQSAS EAVAREIADL IKSKQAQGKH
CVLGLATGSS PVKVYKELIR LHKEEGLSFK NVITFNLDEY YPMEKQDKQS YWQFMHKNLF
DHVDIDPKNI HIPNGTVQAE EVREYCTEYE KAIEQAGGID FQLLGIGRTG HIGFNEPGSH
INSATRMVTL NKVTKTDAAE TFGGYKNVPS KAITMGVGTV MAARRIVLLA WGEPKASIIA
KTIEGEISSQ IPATFLQEHP NTTFVIDQTA ASELTRNKTP WLVGEYDFKN NQEEIARAVI
WLCEKLGKTI LGLREEDYLE NGLGNLLQEK SAYDLNIDIF NRIQRAITGW PGGKPNADDK
YRPEREVPHK KRVIIFSPHP DDDVISMGGT FDRLVEQGHE VHIAYQTSGS TAVADTEALR
FVEVAHDMLL GKTDVSHLEE VIKVLRNKKA GDKETLDVWK LKGNIRRHEC YGATRYYNVP
DENLHFLNLP FYETQAVEKQ PIGEADIKII EDLIREVKPH QIYAAGDLAD PHGTHKVCLD
GIFAALERLK GEDYMKDCWV WLYRGAWHEW DVHEMEMIVP MTRDQVLRKR QAIFFHQSQK
DGAMYMGSDM REFWQRAEER NSDTAKRLHK LGLAKYEAME AFRRYFF
//
