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Database: UniProt
Entry: S5RJ09_9STRE
LinkDB: S5RJ09_9STRE
Original site: S5RJ09_9STRE 
ID   S5RJ09_9STRE            Unreviewed;       450 AA.
AC   S5RJ09;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
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=KE3_1343 {ECO:0000313|EMBL:AGS05821.1};
OS   Streptococcus lutetiensis 033.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1076934 {ECO:0000313|EMBL:AGS05821.1, ECO:0000313|Proteomes:UP000015268};
RN   [1] {ECO:0000313|EMBL:AGS05821.1, ECO:0000313|Proteomes:UP000015268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=033 {ECO:0000313|EMBL:AGS05821.1,
RC   ECO:0000313|Proteomes:UP000015268};
RX   PubMed=23782707; DOI=10.1186/1471-2180-13-141;
RA   Jin D., Chen C., Li L., Lu S., Li Z., Zhou Z., Jing H., Xu Y., Du P.,
RA   Wang H., Xiong Y., Zheng H., Bai X., Sun H., Wang L., Ye C., Gottschalk M.,
RA   Xu J.;
RT   "Dynamics of fecal microbial communities in children with diarrhea of
RT   unknown etiology and genomic analysis of associated Streptococcus
RT   lutetiensis.";
RL   BMC Microbiol. 13:141-141(2013).
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}.
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DR   EMBL; CP003025; AGS05821.1; -; Genomic_DNA.
DR   RefSeq; WP_020917070.1; NC_021900.1.
DR   AlphaFoldDB; S5RJ09; -.
DR   GeneID; 58528492; -.
DR   KEGG; slu:KE3_1343; -.
DR   PATRIC; fig|1076934.5.peg.1304; -.
DR   HOGENOM; CLU_016950_7_0_9; -.
DR   Proteomes; UP000015268; 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   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; PHOSPHOGLUCOSAMINE MUTASE FAMILY PROTEIN; 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}.
FT   DOMAIN          3..134
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          162..253
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          257..365
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          373..444
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   ACT_SITE        101
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         101
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         240
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         242
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   450 AA;  48346 MW;  7A6A61726632C508 CRC64;
     MGKYFGTDGV RGEANVELTP ELAFKLGRFG GYVLSQHETG RPKVFVARDT RISGEMLESA
     LVAGLLSVGI EVYKLGVLAT PGVSYLVRTE KASAGVMISA SHNPAQDNGI KFFGGDGFKL
     ADDQELEIEA LLDAPEDTLP RPSADGLGTL VDYPEGLRKY EKFLVSTGIS LEGMKVALDT
     ANGSASVSAR DIFLDLDADI TVIGENPDGL NINDGVGSTH PEQLQELVKE SGAAVGLAFD
     GDSDRLIAVD ENGEIVDGDK VMYIIGKYLS ERGQLAHNTI VTTVMSNLGF HKALDREGIN
     KAITAVGDRY VVEEMRKSGF NLGGEQSGHV IIMDYNTTGD GQLTGIQLVK VMKETGKPLS
     ELAAEVTIYP QKLVNIRVEN SMKSKAMEVP AIAEIISKME EEMNGNGRIL VRPSGTEPLL
     RVMAEAPTDE EVDYYVNTIA DVVRNEIGID
//
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