ID A0A0J0YMU3_9FLAO Unreviewed; 645 AA.
AC A0A0J0YMU3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=AB674_01695 {ECO:0000313|EMBL:KLT71469.1};
OS Flavobacterium sp. ABG.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1423322 {ECO:0000313|EMBL:KLT71469.1, ECO:0000313|Proteomes:UP000036173};
RN [1] {ECO:0000313|EMBL:KLT71469.1, ECO:0000313|Proteomes:UP000036173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABG {ECO:0000313|EMBL:KLT71469.1,
RC ECO:0000313|Proteomes:UP000036173};
RA Gimbel A.B., Miller J.R., Newman J.D.;
RT "Flavobacterium sp. ABG.";
RL Submitted (JUN-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 (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:KLT71469.1}.
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DR EMBL; LEKS01000002; KLT71469.1; -; Genomic_DNA.
DR RefSeq; WP_047773744.1; NZ_LEKS01000002.1.
DR AlphaFoldDB; A0A0J0YMU3; -.
DR STRING; 1423322.AB674_01695; -.
DR PATRIC; fig|1423322.9.peg.352; -.
DR OrthoDB; 9791139at2; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000036173; 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, ECO:0000313|EMBL:KLT71469.1}.
FT DOMAIN 38..258
FT /note="Glucosamine/galactosamine-6-phosphate isomerase"
FT /evidence="ECO:0000259|Pfam:PF01182"
FT ACT_SITE 97
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
FT ACT_SITE 170
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
FT ACT_SITE 175
FT /note="For ring-opening step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
SQ SEQUENCE 645 AA; 72917 MW; 0269F8A3B9320F33 CRC64;
MKSALEIKPD ISYKSAGKFE ETRFEKIHNE IFKNSTEASL IVAQEIAQLI RSKQEKDKSC
VLGLATGSSP IKVYEELVRM HREEGLSFSN VITFNLDEYY PMTKENNQSY HHFMHQHLFN
HIDINPDNVN IPDGTIAIDE LNQYCIDYEM NIKNAGGLDF QLLGIGRTGH VGFNEPGSHI
NSGTRIITLD HITRVDASSD FNGIDNVPKR AITMGVSTIM RSKRIVLMAW GQNKADIIKR
TVQGDISSEV PATFLQNHPN ATFVLDQSAA SELTRFKTPW LVGECIWTQE LKSKAIVWLC
QKTKQSILKL TDRDYNNNGM SDLLAQEGSA YDLNINMFNV LQHTITGWPG GKPNTDDSHR
PERANPAKKR VILFSPHPDD DVISMGGTFS KLIKQGHDVH VVYQTSGNIA VTDDEALKFA
EVGSDFIGAG AADINFKSVI EFLNNKSENQ IDSLEVRKLK GLIRRRESYA ATRYIGLKDE
NTHFLDLPFY ETGQVKKNPL GPDDIAIVKD IIAKIKPHQV FAAGDLADPH GTHEVCLNAI
FAAMAALKPQ AYMDDCWLWL YRGAWHEWDI HEIDMAVPLS PSEVLLKRHA ILYHQSQKDR
VMFQGNDSRE FWVRAEDRNK NTAVLYDDLG LAEYEAIEAF KRFDY
//
