ID A0A2P7ECZ7_9SYNE Unreviewed; 458 AA.
AC A0A2P7ECZ7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Phosphoglucosamine mutase {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327};
DE EC=5.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327};
GN Name=glmM {ECO:0000256|HAMAP-Rule:MF_01554};
GN ORFNames=C7K08_09720 {ECO:0000313|EMBL:PSI01095.1};
OS Synechococcus lacustris str. Tous.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1910958 {ECO:0000313|EMBL:PSI01095.1, ECO:0000313|Proteomes:UP000240206};
RN [1] {ECO:0000313|Proteomes:UP000240206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tous {ECO:0000313|Proteomes:UP000240206};
RA Cabello-Yeves P.J., Picazo A., Camacho A., Callieri C., Rosselli R.,
RA Roda-Garcia J., Coutinho F.H., Rodriguez-Valera F.;
RT "Ecological and genomic features of two cosmopolitan and abundant
RT freshwater picocyanobacteria.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC glucosamine-1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01554,
CC ECO:0000256|RuleBase:RU004327}.
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:0000256|HAMAP-Rule:MF_01554,
CC ECO:0000256|RuleBase:RU004327};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01554};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01554};
CC -!- PTM: Activated by phosphorylation. {ECO:0000256|HAMAP-Rule:MF_01554}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|HAMAP-Rule:MF_01554,
CC ECO:0000256|RuleBase:RU004326}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSI01095.1}.
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DR EMBL; PXVC01000050; PSI01095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P7ECZ7; -.
DR STRING; 1910958.BTM30_08600; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000240206; Unassembled WGS sequence.
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 Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 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 NCBIfam; TIGR01455; glmM; 1.
DR PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
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; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01554};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01554};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01554};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_01554}; Reference proteome {ECO:0000313|Proteomes:UP000240206}.
FT DOMAIN 18..142
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 167..261
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 265..373
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 381..450
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT ACT_SITE 111
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 111
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ SEQUENCE 458 AA; 48163 MW; B87A2FF74F6E7940 CRC64;
MADLATHPVG QPFSAGVSFG TDGIRGLVGG LMTPALAMQV GYWGGLVLQG EGPVLIGRDS
RSSGWMLSAA LEAGLTAAGR EVWNLGLCPT PAVARLVQQQ GAAGGVMVSA SHNPPADNGI
KLFAAGGSKL ARQQQELIEA GLRGELPAAA NRCGSSHQRS DLLAIYRQLL REGLADNQLS
GRRIVLDLCW GSATACSSEL FRSLGAEVIE LHGSPDGNAI NVGCGSTHLA PLQEAVRQSG
AELGFAFDGD ADRVLAVDGE GRLVDGDHIL FMWGSALAAA GQLPKQLLVA TVMSNLGFER
AWRSGGGQLE RTAVGDQYVH EAMQNLGAAL GGEQSGHILC AHHGLTGDGL LTALQLAALL
KPGESLADRR NQSFVSYPQR LKNVRVANRE RRQQWQQCDP LAQAVARAEA EMAGEGRVLV
RASGTEPLLR VMVEASSQAV VDHWIENLAA IAERELNH
//
