ID A0AAN5YDV8_9LACT Unreviewed; 235 AA. AC A0AAN5YDV8; DT 02-OCT-2024, integrated into UniProtKB/TrEMBL. DT 02-OCT-2024, sequence version 1. DT 27-NOV-2024, entry version 2. 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=FPV22_02310 {ECO:0000313|EMBL:KAF3303479.1}, FPV22_02320 GN {ECO:0000313|EMBL:QEM59078.1}; OS Carnobacterium sp. PL26RED25. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae; OC Carnobacterium. OX NCBI_TaxID=2592352 {ECO:0000313|EMBL:KAF3303479.1, ECO:0000313|Proteomes:UP000323114}; RN [1] {ECO:0000313|EMBL:QEM59078.1, ECO:0000313|Proteomes:UP000323114} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PL26RED25 {ECO:0000313|EMBL:QEM59078.1, RC ECO:0000313|Proteomes:UP000323114}; RA Korzeniowski K., Mukherjee S., De Meester L., Souffreau C.; RT "Genome Sequences of Carnobacterium sp. strains isolated from freshwater RT ponds in Belgium."; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KAF3303479.1, ECO:0000313|Proteomes:UP000323114} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PL26RED25 {ECO:0000313|EMBL:KAF3303479.1, RC ECO:0000313|Proteomes:UP000323114}; RA Korzeniowski K., Mukherjee S., Souffreau C., De Meester L.; RT "Draft genomes of Carnobacterium sp. 1290."; RL Submitted (NOV-2019) 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; WVEP01000002; KAF3303479.1; -; Genomic_DNA. DR EMBL; CP041942; QEM59078.1; -; Genomic_DNA. DR Proteomes; UP000323114; Chromosome. DR Proteomes; UP000323114; Unassembled WGS sequence. DR CDD; cd01399; GlcN6P_deaminase; 1. DR FunFam; 3.40.50.1360:FF:000003; Glucosamine-6-phosphate deaminase; 1. DR Gene3D; 3.40.50.1360; -; 1. DR HAMAP; MF_01241; GlcN6P_deamin; 1. DR InterPro; IPR006148; Glc/Gal-6P_isomerase. DR InterPro; IPR004547; Glucosamine6P_isomerase. DR InterPro; IPR037171; NagB/RpiA_transferase-like. DR PANTHER; PTHR11280; GLUCOSAMINE-6-PHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR11280:SF5; GLUCOSAMINE-6-PHOSPHATE ISOMERASE; 1. DR Pfam; PF01182; Glucosamine_iso; 1. DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP- KW Rule:MF_01241}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_01241}. FT DOMAIN 8..218 FT /note="Glucosamine/galactosamine-6-phosphate isomerase" FT /evidence="ECO:0000259|Pfam:PF01182" FT ACT_SITE 62 FT /note="Proton acceptor; for enolization step" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" FT ACT_SITE 128 FT /note="For ring-opening step" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" FT ACT_SITE 130 FT /note="Proton acceptor; for ring-opening step" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" FT ACT_SITE 135 FT /note="For ring-opening step" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01241" SQ SEQUENCE 235 AA; 25692 MW; E02724058D61F199 CRC64; MDIKIFDTAK EASKEVLHEF DQALASGATT FGLATGSTPE DLYEYLTSSN LDFSNATALN LDEYFGLPAN HPESYATFMD KHLFSKKPFK ETFIPNGLAT DVEAEITRYN TLLDEHPIDL QILGIGQNAH IGFNEPGSSR HTKTQLVDLA ESTIQANARF FDSVEDVPTK AFSMGLASIM QSKRILLLAF GESKAQAVKD MVEGPVTEDV PASLLQEHPN VTVYLDSAAA SLLNK //