(data stored in SCRATCH zone)

SWISSPROT: D6XX57_BACIE

ID   D6XX57_BACIE            Unreviewed;       453 AA.
AC   D6XX57;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 66.
DE   RecName: Full=Phosphoglucosamine mutase {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327, ECO:0000256|SAAS:SAAS00358419};
DE            EC=5.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327, ECO:0000256|SAAS:SAAS00078300};
GN   Name=glmM {ECO:0000256|HAMAP-Rule:MF_01554};
GN   OrderedLocusNames=Bsel_0374 {ECO:0000313|EMBL:ADH97914.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97914.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97914.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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, ECO:0000256|SAAS:SAAS00566919}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucosamine 1-phosphate = D-glucosamine 6-
CC         phosphate; Xref=Rhea:RHEA:23424, ChEBI:CHEBI:58516,
CC         ChEBI:CHEBI:58725; EC=5.4.2.10; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01554, ECO:0000256|RuleBase:RU004327,
CC         ECO:0000256|SAAS:SAAS01123721};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01554};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01554};
CC   -!- PTM: Activated by phosphorylation. {ECO:0000256|HAMAP-
CC       Rule:MF_01554}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004326,
CC       ECO:0000256|SAAS:SAAS00551227}.
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DR   EMBL; CP001791; ADH97914.1; -; Genomic_DNA.
DR   RefSeq; WP_013171343.1; NC_014219.1.
DR   STRING; 439292.Bsel_0374; -.
DR   EnsemblBacteria; ADH97914; ADH97914; Bsel_0374.
DR   KEGG; bse:Bsel_0374; -.
DR   eggNOG; ENOG4107QJF; Bacteria.
DR   eggNOG; COG1109; LUCA.
DR   HOGENOM; HOG000268678; -.
DR   KO; K03431; -.
DR   OMA; MFGEEYT; -.
DR   OrthoDB; 1265792at2; -.
DR   BioCyc; BSEL439292:G1GLR-404-MONOMER; -.
DR   Proteomes; UP000000271; 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;
DR   PRODOM; D6XX57.
DR   SWISS-2DPAGE; D6XX57.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01554,
KW   ECO:0000256|RuleBase:RU004327, ECO:0000256|SAAS:SAAS01085081};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01554,
KW   ECO:0000256|RuleBase:RU004326, ECO:0000256|SAAS:SAAS00436074};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01554,
KW   ECO:0000256|RuleBase:RU004326, ECO:0000256|SAAS:SAAS00436123};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01554};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN        4    135       PGM_PMM_I. {ECO:0000259|Pfam:PF02878}.
FT   DOMAIN      161    257       PGM_PMM_II. {ECO:0000259|Pfam:PF02879}.
FT   DOMAIN      261    373       PGM_PMM_III. {ECO:0000259|Pfam:PF02880}.
FT   DOMAIN      377    443       PGM_PMM_IV. {ECO:0000259|Pfam:PF00408}.
FT   COILED      120    140       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    100    100       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01554}.
FT   METAL       100    100       Magnesium; via phosphate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01554}.
FT   METAL       244    244       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
FT   METAL       246    246       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
FT   METAL       248    248       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
FT   MOD_RES     100    100       Phosphoserine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
SQ   SEQUENCE   453 AA;  48881 MW;  F565EE23208401AD CRC64;
     MGKFFGTDGV RGIANKELTP ELAFKLGRFG GYVLTKETEK PKILIGRDPR ISGPMLESAL
     IAGLLSMGAE VMRLGVITTP GVAYLTKALS ADAGVMISAS HNPVEDNGIK FFGPDGFKLV
     DEQEEEIERL LHQEDDMEDD LPRPVGGEIG TVSDYFEGGQ KYLRFLKQTL SEDFSGLKIA
     IDCAHGAASS LANHLFADLE AEDIFCIGSS PNGVNINAGV GSTHPEGLVD LVKEKGADIG
     LAFDGDADRL IAVDEKGNIV DGDQIMYITA KYLRDNGRLV DDTVVSTVMS NLGFYKALEE
     AGIQTKQTAV GDRYVMEEMR KGNYSLGGEQ SGHIIFLEHS TTGDGLLSGI QLVQIMKATG
     KTLSELASEW SHYPQKLVNV RVADKHALHN NDVIADEIRA VEQGMNGEGR ILVRPSGTEP
     LVRVMAEAPS REKCEEIVDG IVGVVKRELG SIE
//

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