GLMM_ALIF1
ID GLMM_ALIF1 Reviewed; 445 AA.
AC Q5E7M0;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 99.
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=VF_0481;
GN ORFNames=VF0482;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=18366731; DOI=10.1186/1471-2164-9-138;
RA Mandel M.J., Stabb E.V., Ruby E.G.;
RT "Comparative genomics-based investigation of resequencing targets in Vibrio
RT fischeri: focus on point miscalls and artefactual expansions.";
RL BMC Genomics 9:138-138(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; CP000020; AAW84976.2; -; Genomic_DNA.
DR RefSeq; WP_011261255.1; NC_006840.2.
DR RefSeq; YP_203864.2; NC_006840.2.
DR AlphaFoldDB; Q5E7M0; -.
DR SMR; Q5E7M0; -.
DR STRING; 312309.VF_0481; -.
DR EnsemblBacteria; AAW84976; AAW84976; VF_0481.
DR KEGG; vfi:VF_0481; -.
DR PATRIC; fig|312309.11.peg.472; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_0_6; -.
DR OMA; VDCGNGM; -.
DR OrthoDB; 1265792at2; -.
DR Proteomes; UP000000537; Chromosome I.
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..445
FT /note="Phosphoglucosamine mutase"
FT /id="PRO_0000147997"
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; 47630 MW; BE79C6CE50BB96BA CRC64;
MAERKYFGTD GVRGLVGQAP ITPDFVMKLG WAAGQVLAKQ GTKKVIIGKD TRISGYMLES
ALEAGLAAAG LQAKFTGPMP TPAVAYLTQT FRAEAGIVIS ASHNPYYDNG IKFFSSEGTK
LPDDVEMAIE AELDKPMTCV ESALLGKASR LNDAAGRYIE FCKSTFPKEL SLAGLKIVID
CANGATYHIA PNVFKELGAE IITIGCEPNG TNINHEVGAT DVRALQAKVV EEKADFGVAF
DGDGDRIIMV DEFGEKVDGD QIAYIIARDA LRRGELKGGV VGTLMTNMGM EVALRNLGIP
FVRSDVGDRY VMEKLLENNW LIGAENSGHV ILLDKVTTGD AIVAALQVIA SIVGSKMSLK
ELCDGMTMFP QILVNVRFAG ENDPLESDAV KAAQADVEAK LGDNGRVLLR KSGTEPLIRV
MVEGEDAELV TQYAQQIADA VKESC
