ID   GLMM_SACD2              Reviewed;         446 AA.
AC   Q21H51;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=Sde_2718;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD81978.1; -; Genomic_DNA.
DR   RefSeq; WP_011469195.1; NC_007912.1.
DR   AlphaFoldDB; Q21H51; -.
DR   SMR; Q21H51; -.
DR   STRING; 203122.Sde_2718; -.
DR   EnsemblBacteria; ABD81978; ABD81978; Sde_2718.
DR   KEGG; sde:Sde_2718; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_7_0_6; -.
DR   OMA; PHNPEPL; -.
DR   OrthoDB; 1265792at2; -.
DR   Proteomes; UP000001947; 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..446
FT                   /note="Phosphoglucosamine mutase"
FT                   /id="PRO_0000301374"
FT   ACT_SITE        105
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         105
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         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   MOD_RES         105
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   446 AA;  47574 MW;  220D79A28B488062 CRC64;
     MARKYFGTDG IRGLVGEGVI TPQFFLQLGW AVGKVLAQQN GDKSGGLVLI GKDTRISGYM
     FESALEAGLI SAGVDVGLLG PMPTPAIAYL TRTFQASAGI VISASHNPYT DNGIKLFNTD
     GTKLPDDVEL AIEDQLDRAM TTASKLGKAR RIADAEGRYI EFCKGSLPWG FNLRGLNIVV
     DCANGATYEV APKVFGELGA NVIPIANKPD GLNINLDCGS TKLNQLQKHV LETGADMGIA
     FDGDGDRVMF VDEKGEVLDG DQLLFIIASH KHKNGGCSGV VGTLMSNFGF ELGLKNQGIP
     FERAKVGDRY VIEAMKNNGW QVGGESSGHI VCSDVTTTGD GIIAALQVLL ALKAEKQSLH
     QLKLRMQKMP QVMINVRVTN KVDLDSHEQV QAAIASAEKR LDGKGRVLLR ASGTEPVIRV
     MVEGQEHQLV ASLAQELADI VGEAVA