GLMM_MICAN
ID GLMM_MICAN Reviewed; 479 AA.
AC B0JVZ6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Phosphoglucosamine mutase {ECO:0000255|HAMAP-Rule:MF_01554};
DE EC=5.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01554};
GN Name=glmM {ECO:0000255|HAMAP-Rule:MF_01554}; OrderedLocusNames=MAE_49170;
OS Microcystis aeruginosa (strain NIES-843 / IAM M-2473).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC Microcystaceae; Microcystis.
OX NCBI_TaxID=449447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-843 / IAM M-247;
RX PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M.,
RA Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.;
RT "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT Microcystis aeruginosa NIES-843.";
RL DNA Res. 14:247-256(2007).
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate;
CC Xref=Rhea:RHEA:23424, ChEBI:CHEBI:58516, ChEBI:CHEBI:58725;
CC EC=5.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01554};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01554};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01554};
CC -!- PTM: Activated by phosphorylation. {ECO:0000255|HAMAP-Rule:MF_01554}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000255|HAMAP-Rule:MF_01554}.
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DR EMBL; AP009552; BAG04739.1; -; Genomic_DNA.
DR RefSeq; WP_012267388.1; NC_010296.1.
DR AlphaFoldDB; B0JVZ6; -.
DR SMR; B0JVZ6; -.
DR STRING; 449447.MAE_49170; -.
DR PaxDb; B0JVZ6; -.
DR PRIDE; B0JVZ6; -.
DR EnsemblBacteria; BAG04739; BAG04739; MAE_49170.
DR KEGG; mar:MAE_49170; -.
DR PATRIC; fig|449447.4.peg.4472; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_0_3; -.
DR OMA; PHNPEPL; -.
DR OrthoDB; 1265792at2; -.
DR BioCyc; MAER449447:MAE_RS21330-MON; -.
DR Proteomes; UP000001510; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05802; GlmM; 1.
DR HAMAP; MF_01554_B; GlmM_B; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR006352; GlmM_bact.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR TIGRFAMs; TIGR01455; glmM; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..479
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_1000087769"
FT ACT_SITE 129
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 129
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ SEQUENCE 479 AA; 51706 MW; CB3C4DEAC964FC2E CRC64;
MVASLSYQNG QKARSHPLLS LAGLIELPPS PLFGTDGIRG QVGELLTAPL ALQIGFWAGQ
VLKNQAGVTK PIIIGQDSRN SSDMLANAIT AGLTWAGIEV WQLGLCPTPC VAYLTRESEA
MGGIMISASH NPPEDNGIKF FDSSGLKLSG TLAGQIEAGL RGNLELADNS VNWGKATFCP
ELIQKYYQAV IASVGTDINL SGLKIVLDLA WGAAVNLAPL VFQTVGAEVI CLHDRADGDR
INVNCGSTHL ESLQAAVINQ QADLGFAFDG DADRVLAVDS QGRVVDGDYI LYFWGRSLLE
AGQLPDGLLV ATVMANLGFE RAWQKLGGQF LRTAVGDQHV QAQMWETGAM LGGEQSGHIL
CHHYGVSGDG MQTALHLAAL VQKSAVSLAN LVDHSFVTYP QILRNVRVED REVRRNWQQC
EPLRREIRKA ETAMAEKGRI LVRASGTEPL IRVMVEAETL ELANFWTERL VAAVRSYLL
