NAGB_MARSD
ID NAGB_MARSD Reviewed; 265 AA.
AC C6C0A2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Glucosamine-6-phosphate deaminase {ECO:0000255|HAMAP-Rule:MF_01241};
DE EC=3.5.99.6 {ECO:0000255|HAMAP-Rule:MF_01241};
DE AltName: Full=GlcN6P deaminase {ECO:0000255|HAMAP-Rule:MF_01241};
DE Short=GNPDA {ECO:0000255|HAMAP-Rule:MF_01241};
DE AltName: Full=Glucosamine-6-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01241};
GN Name=nagB {ECO:0000255|HAMAP-Rule:MF_01241}; OrderedLocusNames=Desal_2921;
OS Maridesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIMB 8403 /
OS VKM B-1763) (Desulfovibrio salexigens).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Maridesulfovibrio.
OX NCBI_TaxID=526222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14822 / DSM 2638 / NCIMB 8403 / VKM B-1763;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.;
RT "Complete sequence of Desulfovibrio salexigens DSM 2638.";
RL Submitted (JUN-2009) 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:0000255|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:0000255|HAMAP-Rule:MF_01241};
CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine 6-
CC phosphate (GlcNAc6P). {ECO:0000255|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:0000255|HAMAP-Rule:MF_01241}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. NagB subfamily. {ECO:0000255|HAMAP-Rule:MF_01241}.
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DR EMBL; CP001649; ACS80973.1; -; Genomic_DNA.
DR RefSeq; WP_015852789.1; NC_012881.1.
DR AlphaFoldDB; C6C0A2; -.
DR SMR; C6C0A2; -.
DR STRING; 526222.Desal_2921; -.
DR EnsemblBacteria; ACS80973; ACS80973; Desal_2921.
DR KEGG; dsa:Desal_2921; -.
DR eggNOG; COG0363; Bacteria.
DR HOGENOM; CLU_049611_0_1_7; -.
DR OMA; FNEPCSS; -.
DR OrthoDB; 1828393at2; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000002601; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; Carbohydrate metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..265
FT /note="Glucosamine-6-phosphate deaminase"
FT /id="PRO_1000214081"
FT ACT_SITE 70
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 139
FT /note="For ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 141
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT ACT_SITE 146
FT /note="For ring-opening step"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 149
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 156
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 158
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 159
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
FT SITE 252
FT /note="Part of the allosteric site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01241"
SQ SEQUENCE 265 AA; 29739 MW; 94F4FB2E61B46AD5 CRC64;
MRLIPLKNNP GWWAARYIAG KIKTFSPSAE NPFVLGLPTG GTPISMYREL INLHRAGEVS
FKHVVTFNMD EYVGLPEDHP QSYHYYMHEN FFNHVDIPKE NINLLDGNAP DPEKECEAYE
QKIINHGGIQ IFVGGVGTDG HIAFNEPASS LSSRTRIKTL TLETRMGNSR FFNNNMEEVP
KYALTVGVGT LLDSKEVIIL ASGLNKALAV SYAVEHGVNH LWTVSALQLH RKGILVCDED
ATMELKVKTL KYFKQIEVDN LQDPK
