SPM_000945


  Uniprot: A0A037UL61
Description: glucosamine-6-phosphate deaminase
EC number: 3.5.99.6
Annotation score: 2 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: Alpha-D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3). {ECO:0000256|HAMAP-Rule:MF_01241, ECO:0000256|SAAS:SAAS00316903}.
Cofactor: 
Enzyme regulation: 
Function [CC]: FUNCTION: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. {ECO:0000256|HAMAP-Rule:MF_01241}.
Pathway: PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5. {ECO:0000256|HAMAP-Rule:MF_01241}.
Active site: ACT_SITE 67 67 Proton acceptor; for enolization step. {ECO:0000256|HAMAP-Rule:MF_01241}.; ACT_SITE 135 135 For ring-opening step. {ECO:0000256|HAMAP-Rule:MF_01241}.; ACT_SITE 137 137 Proton acceptor; for ring-opening step. {ECO:0000256|HAMAP-Rule:MF_01241}.; ACT_SITE 142 142 For ring-opening step. {ECO:0000256|HAMAP-Rule:MF_01241}.
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: 
Site: 
Gene names (primary): nagB
Gene names (synonym): 
Mass: 27,251
Subunit structure [CC]: 
Gene ontology (GO): glucosamine-6-phosphate deaminase activity [GO:0004342]; hydrolase activity [GO:0016787]; carbohydrate metabolic process [GO:0005975]; N-acetylglucosamine metabolic process [GO:0006044]
Gene ontology IDs: GO:0004342; GO:0005975; GO:0006044; GO:0016787
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. NagB subfamily. {ECO:0000256|HAMAP-Rule:MF_01241}.
Protein families: Glucosamine/galactosamine-6-phosphate isomerase family, NagB subfamily
Coiled coil: 
Domain [FT]: DOMAIN 14 228 Glucosamine_iso. {ECO:0000259|Pfam:PF01182}.
Motif: 
Region: 
EMBL: AGBZ02000001
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: KAI92649
UniPathway: 
CDD: 
Gene3D: 
HAMAP: 
InterPro: MF_01241
PANTHER: IPR006148;IPR004547;IPR018321
PIRSF: PTHR11280
PRINTS: 
PROSITE: 
Pfam: PS01161
ProDom: PF01182
SMART: 
SUPFAM: 
TIGRFAMs: 
178433-179180(-)

>nucleotide sequence
TTAACCAAGATTAATCCCTCTTGTTTGCAGTAATCCAGCAGCTGCTTTATCAACCACAAC
AGTAACATCTTGATGCATTTGTAAAGCCGTACAAGGTCATAAGTTGCTAATTTCACCTTC
AACTAGTTGTTTAACCGCGTGTGCTTTATTTGGACCATTGGCAATTAAAATAATTTTTTT
TGCATTTAAAATTGATTTAATTCCCATTGAAACTGCTTGGTGAGGAACATCACCTGCTGA
AGCAAAAAAACGAGCATTAGTTTCAATTGTTGAAGGAACTAAATCAACAACACCTGTTAA
AGAATTAAAATCTGCTGGTGGTTCATTAAAGCCAATATGTCCATTAGTACCAAGTCCTAA
TAATTGTAAGTCAATTCCTCCCGCTTTTGCAATCAAACTATCATATTCTTTCGCATAGTC
AATATAATTACCTGTACCTAATGGGACATAAGTATGTTTTTTATCAATATTTAAGTGATT
AAATAATTTTTCATTCATGAAATAACGATAACTTTGTGGATGGTTTGGTTCTAAACCAAT
GTATTCATCTAAGTTAAAAGTCGTTACTTTACTTCAGTCTGTCTTATTTTTTTTATAATC
TTCAATAATATATTGATAAGTTGTTTCTGGTGATGAACCAGTTGCTAAACCAAAAACAAC
TTTTGGATTTTGTTGCACATAATTCACAAAGATTTGCCCAACAACTTTTCCAATTGCATT
TTTATCTTCAACAATAATTAATTTCAT


>protein sequence
MKLIIVEDKNAIGKVVGQIFVNYVQQNPKVVFGLATGSSPETTYQYIIEDYKKNKTDWSK
VTTFNLDEYIGLEPNHPQSYRYFMNEKLFNHLNIDKKHTYVPLGTGNYIDYAKEYDSLIA
KAGGIDLQLLGLGTNGHIGFNEPPADFNSLTGVVDLVPSTIETNARFFASAGDVPHQAVS
MGIKSILNAKKIILIANGPNKAHAVKQLVEGEISNLWPCTALQMHQDVTVVVDKAAAGLL
QTRGINLG






















© Fisunov Lab of Proteomics, 2016.