ID A0A1I5U4B8_9BACT Unreviewed; 632 AA.
AC A0A1I5U4B8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN05444277_10360 {ECO:0000313|EMBL:SFP90145.1};
OS Parafilimonas terrae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Parafilimonas.
OX NCBI_TaxID=1465490 {ECO:0000313|EMBL:SFP90145.1, ECO:0000313|Proteomes:UP000199031};
RN [1] {ECO:0000313|EMBL:SFP90145.1, ECO:0000313|Proteomes:UP000199031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28286 {ECO:0000313|EMBL:SFP90145.1,
RC ECO:0000313|Proteomes:UP000199031};
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; FOXQ01000003; SFP90145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5U4B8; -.
DR STRING; 1465490.SAMN05444277_10360; -.
DR OrthoDB; 9791139at2; -.
DR UniPathway; UPA00629; UER00684.
DR Proteomes; UP000199031; 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; IPR018321; Glucosamine6P_isomerase_CS.
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.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01241};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01241};
KW Reference proteome {ECO:0000313|Proteomes:UP000199031}.
FT DOMAIN 17..241
FT /note="Glucosamine/galactosamine-6-phosphate isomerase"
FT /evidence="ECO:0000259|Pfam:PF01182"
FT ACT_SITE 78
FT /note="Proton acceptor; for enolization step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
FT ACT_SITE 149
FT /note="For ring-opening step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
FT ACT_SITE 151
FT /note="Proton acceptor; for ring-opening step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
FT ACT_SITE 156
FT /note="For ring-opening step"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241"
SQ SEQUENCE 632 AA; 71713 MW; 98E7F2B337FA39DD CRC64;
MVDSFEKIPV EIFPTSTEGS HYAAGEIAKL IRQKQEENKP CVLGLATGST PISMYKELVR
MHKEEGLSFK NVITFNLDEY FPITKTAFQS YWSFMHRHLF DHIDIKPENI HIPNGDLSKE
EAKKHCIEYE QMIDDAGGID LQVLGIGNNG HIGFNEPGSS IFSKTHITNL DNSTRVANAR
EFQNISKVPR LALTMGISTI MKAKRVLLMA WGFKAPIIAK AMEGNVTEQV PASILQQHNN
CTFILDEQAA SELARFKSPW LTGEIEWTPK IIKRAVVNLA LKLNKPVLSL TTLDYNENGL
GDLLVEKGDA YEINLQVYYL LRDSITGWPG GKPNVDLPTH PERSDPYPKR VIIFSPHPDD
DIISMGGTFM RLHDQGHDVH VAYQTSGNIA VTDEFVTRFL DFAVGFQDLF DMDNKKSTKI
LEDAQHYLAS KKSGGVDTPE IRAIKGLIRR CEAKATCKYV GLTEGHWHFQ NLPFYETGTI
EKKPMGEEDI KLTMQLLREI KPHQVYAAGD LADPHGTHKV CLDIVFESLR RIKAEGDEWI
NDCWLWLYKG AWQEWDIADI EMAIPMSPDQ VVKKRFGIFI HQSQKDAVPF QGTDTREFWQ
RAEDRNANTA NLYSALGLTK YAAMEAFVRW MY
//
