GLMM1_SHESR
ID GLMM1_SHESR Reviewed; 445 AA.
AC Q0HXS0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phosphoglucosamine mutase 1 {ECO:0000255|HAMAP-Rule:MF_01554};
DE EC=5.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01554};
GN Name=glmM1 {ECO:0000255|HAMAP-Rule:MF_01554};
GN OrderedLocusNames=Shewmr7_1086;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000444; ABI42085.1; -; Genomic_DNA.
DR RefSeq; WP_011625493.1; NC_008322.1.
DR AlphaFoldDB; Q0HXS0; -.
DR SMR; Q0HXS0; -.
DR EnsemblBacteria; ABI42085; ABI42085; Shewmr7_1086.
DR KEGG; shm:Shewmr7_1086; -.
DR HOGENOM; CLU_016950_7_0_6; -.
DR OMA; VDCGNGM; -.
DR OrthoDB; 1265792at2; -.
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.
FT CHAIN 1..445
FT /note="Phosphoglucosamine mutase 1"
FT /id="PRO_0000305677"
FT ACT_SITE 102
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 102
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 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ SEQUENCE 445 AA; 47598 MW; AFA488DFC0D787B8 CRC64;
MSERKFFGTD GIRGKVGSGQ MTPELALKLG WAAGRVLSRS GTNKVIIGKD TRISGYMFES
ALEAGLSAAG LNVMLMGPMP TPAVAYLTRT FRAEAGVVIS ASHNPYYDNG IKFFSNDGSK
LDDNLELEIE AELEKPLECV ESHLLGKVSR IEDARGRYIE YCKGNFPADQ TLTGLKIVVD
CAHGATYHIA PAVFRELGAE VIAIGDKPNG VNINDKVGAT SMAKICETVL TEGADLGIAL
DGDGDRIMMV NSRGEVIDGD QILYILACDA KARGVLRGGV VGTLMSNLGL DLALQALDIP
FARSKVGDRY VMELLKELDW RIGGENSGHI LNLDHGTTGD GIVAGILVLA AMRRQNATLE
QLTAPMEMLP QVLVNVRFEG EHDPLSSDKV KAAQAQVESQ LGARGRVLLR KSGTEPLIRV
MVEGDDHNTV LAHANLIADA VKSAS