(data stored in ACNUC7421 zone)

SWISSPROT: GLMM_ALCBS

ID   GLMM_ALCBS              Reviewed;         444 AA.
AC   Q0VSS6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   11-DEC-2019, entry version 85.
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=ABO_0324;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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}.
DR   EMBL; AM286690; CAL15772.1; -; Genomic_DNA.
DR   RefSeq; WP_011587620.1; NC_008260.1.
DR   SMR; Q0VSS6; -.
DR   STRING; 393595.ABO_0324; -.
DR   PRIDE; Q0VSS6; -.
DR   EnsemblBacteria; CAL15772; CAL15772; ABO_0324.
DR   KEGG; abo:ABO_0324; -.
DR   eggNOG; ENOG4107QJF; Bacteria.
DR   eggNOG; COG1109; LUCA.
DR   HOGENOM; HOG000268678; -.
DR   KO; K03431; -.
DR   OMA; VMIHEAD; -.
DR   OrthoDB; 1265792at2; -.
DR   BioCyc; ABOR393595:ABO_RS01645-MONOMER; -.
DR   Proteomes; UP000008871; 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; Q0VSS6.
DR   SWISS-2DPAGE; Q0VSS6.
KW   Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT   CHAIN           1..444
FT                   /note="Phosphoglucosamine mutase"
FT                   /id="PRO_0000301272"
FT   ACT_SITE        101
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   METAL           101
FT                   /note="Magnesium; via phosphate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   METAL           239
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   METAL           241
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   METAL           243
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
FT   MOD_RES         101
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   444 AA;  47658 MW;  8A4D4CC3BFD2CD66 CRC64;
     MTRKYFGTDG VRGTVGEFPI TPDFVLKLGW AAGKVLGARG GSKILIGKDT RISGYMFESA
     LEAGISAAGV DVRLLGPLPT PGIAYLTRTL SAQAGIVISA SHNPYTDNGI KFFGADGRKL
     NDEIELEIER LLDEQMSVVS TDQIGKVRRI DDARGRYIEF CKSTAPGLDL NGMKIVVDTA
     NGAAYHIAPD VFEELGATVV PLANQPDGFN INRDCGSTHP EALQRKVVEE KADLGVALDG
     DADRLLMVDH AGNLVDGDQL LFVVARDRKE NGAEMDGVVG TLMSNFGLEL ALQAEGIEFV
     RAKVGDRYVM EQLDKRGWNI GGESSGHLVC LDCTTTGDGT VSALQVLAAL SRRKQGLAES
     VADVSMLPQK MINVRGPNRD GFMENGDVQA AMADVEDRLA GNGRILLRPS GTEPLVRVMI
     EGKDVDRVES LCRELAEVVE KAIN
//

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