ACL_RS05130
  | Uniprot: A9NH17
Description: phosphoglucosamine mutase EC number: 5.4.2.10 Annotation score: 2 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. {ECO:0000256|SAAS:SAAS00358409}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|SAAS:SAAS00609101}; Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. {ECO:0000256|SAAS:SAAS00551243}. Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: Site: Gene names (primary): glmM Gene names (synonym): Mass: 48,102 Subunit structure [CC]: Gene ontology (GO): magnesium ion binding [GO:0000287]; phosphoglucosamine mutase activity [GO:0008966]; carbohydrate metabolic process [GO:0005975] Gene ontology IDs: GO:0000287; GO:0005975; GO:0008966 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000256|RuleBase:RU004326, ECO:0000256|SAAS:SAAS00551227}. Protein families: Phosphohexose mutase family Coiled coil: Domain [FT]: DOMAIN 4 129 PGM_PMM_I. {ECO:0000259|Pfam:PF02878}.; DOMAIN 158 243 PGM_PMM_II. {ECO:0000259|Pfam:PF02879}.; DOMAIN 247 355 PGM_PMM_III. {ECO:0000259|Pfam:PF02880}.; DOMAIN 364 411 PGM_PMM_IV. {ECO:0000259|Pfam:PF00408}. Motif: Region: EMBL: CP000896 ProteinModelPortal: A9NH17 MEROPS: EnsemblBacteria KO: ABX81647 UniPathway: K03431 CDD: Gene3D: cd05802 HAMAP: 3.30.310.50;3.40.120.10 InterPro: PANTHER: IPR005844;IPR016055;IPR005845;IPR005846;IPR005843;IPR016066;IPR005841;IPR006352 PIRSF: PRINTS: PROSITE: PR00509 Pfam: PS00710 ProDom: PF02878;PF02879;PF02880;PF00408 SMART: SUPFAM: TIGRFAMs: SSF53738;SSF55957 |
1065149-1066460(-) >nucleotide sequence TAAGATATCTTGACAACTTATTGTAACACGAACTAAAGGTTCTGTACCACTAGGACGTAC TAATAATAAAGAATCTTCTGATAGATTTCTTCTAACTTCTTCTACTAGTTTAATTATTTC GGGATGTTTGAGTACTTCTTTATCAACATTTTTGATGTTGACCATTTTTTGAGGATACAT TTCTACTTCCTTTGTATAATCTTTTAGTGATGTTTTATGTTCTTCTAAGATCTTTAGTAT ATAAACACCTGCAAATAAACCATCACCTGAAGGCAGTAAGTCATTTATGATGATATGTCC TGAATTTTCTCCACCTATGCTTAAATCGTGATTCATAATTTCTTCAGATACATATTTATC TCCTACTGGAGTTTGAAGTACTTTGATACCTAATGTTTTAAATGCTTTAAGCATACCAGG ATTACTCATTTGAGTTAAGACTACTGTATCTTTTTTAAGTTTTCCTTTAGATTTTAAGTA CTTAGCTATGATGTAGACAATGTAGTCTCCATCAAATGTAGTACCATCCTTGTCTACAAC TAAAAGACGATCCCCATCACCATCAAAAGATAGTCCAATGTCTGAACCGTTACTTTTAAC TGCATTAATGATAGATTCTAAGTGAGTTGATCCTACATTTAAGTTAATGTTTAACCCATC TGGCCTGTTACCTATTTGATAGGTATGTGATGCAAAAGACTCTATTACTTTTTTAGAAAT AAGATAGTTAGCTCCATTTGCAGAATCATAGGTTATTTTCATAGATGTTTTAGGAATATT TAAATCTTGATAGACATTTATATAAATATCTTCTACATCATGTGTTATTTCTATTGAACC TAGTTTCGTTGAAGATAAAACCTCATTATCATCAATGTAGGTTTCTAAATTAAGTTCTTC TTCATCAAGCATTTTATAACCTGATTTAATGACTTTAATACCATTATCAGTATATGGGTT ATGAGATGCAGTGATCATAACTCCTATGATATCTTTCACTTTAGAGTAATAAGCAATCAT AGGTGTTGAAACAACACCTGCAATTTTTACATTTACTCCAGCTAGTGCTGCACCGTATGC AACACCATATGCAAGCATGTTTGAAGATAGTCTAGTATCTTGACCAATGATGATTTCACT AGGACTAAACTTTTTAGCTATGGCTTGACCTAATTTAAACGCTAGTTTTGAATTTAATTT TTCAAAAGCGATACCGCGTATCCCATCGGTACCAAAATAATTATTTTTCAT >protein sequence AALAGVNVKIAGVVSTPMIAYYSKVKDIIGVMITASHNPYTDNGIKVIKSGYKMLDEEEL NLETYIDDNEVLSSTKLGSIEITHDVEDIYINVYQDLNIPKTSMKITYDSANGANYLISK KVIESFASHTYQIGNRPDGLNINLNVGSTHLESIINAVKSNGSDIGLSFDGDGDRLLVVD KDGTTFDGDYIVYIIAKYLKSKGKLKKDTVVLTQMSNPGMLKAFKTLGIKVLQTPVGDKY VSEEIMNHDLSIGGENSGHIIINDLLPSGDGLFAGVYILKILEEHKTSLKDYTKEVEMYP QKMVNIKNVDKEVLKHPEIIKLVEEVRRNLSEDSLLLVRPSGTEPLVRVTISCQDILELD KYMGLLVTKIQNLGRL |
© Fisunov Lab of Proteomics, 2016.