(data stored in ACNUC7421 zone)

HOGENOM: POLSQ_1_PE1005

ID   POLSQ_1_PE1005                       STANDARD;      PRT;   450 AA.
AC   POLSQ_1_PE1005; A4SXL3;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Phosphoglucosamine mutase; EC=5.4.2 10; (POLSQ_1.PE1005).
GN   Name=glmM; OrderedLocusNames=Pnuc_1011;
OS   POLYNUCLEOBACTER NECESSARIUS SUBSP. ASYMBIOTICUS QLW-P1DMWA-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS POLSQ_1.PE1005.
CC       Polynucleobacter necessarius subsp. asymbioticus QLW-P1DMWA-1, complete
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:GLMM_POLSQ
CC   -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to
CC       glucosamine-1-phosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 1-phosphate = D-
CC       glucosamine 6-phosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PTM: Activated by phosphorylation (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABP34227.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000268678 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A4SXL3; -.
DR   EMBL; CP000655; ABP34227.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_001155791.1; NC_009379.1.
DR   ProteinModelPortal; A4SXL3; -.
DR   STRING; A4SXL3; -.
DR   GeneID; 5053308; -.
DR   GenomeReviews; CP000655_GR; Pnuc_1011.
DR   KEGG; pnu:Pnuc_1011; -.
DR   eggNOG; COG1109; -.
DR   PhylomeDB; A4SXL3; -.
DR   ProtClustDB; PRK10887; -.
DR   BioCyc; PSP312153:PNUC_1011-MON; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   InterPro; IPR006352; GlmM.
DR   Gene3D; G3DSA:3.40.120.10; A-D-PHexomutase_a/b/a-I/II/III; 3.
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; A-D-PHexomutase_a/b/a-I/II/III; 3.
DR   TIGRFAMs; TIGR01455; GlmM; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
DR   HOGENOMDNA; POLSQ_1.PE1005; -.
KW   phosphoglucosamine mutase;
KW   Complete proteome; Isomerase; Magnesium; Metal-binding;
KW   Phosphoprotein.
SQ   SEQUENCE   450 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTVMKKQYFG TDGIRGEVGK FPIVPEFMTR LGYAAGKVLT KDAKPHERCK VLIGKDTRVS
     GYLLEAALEA GFAAAGVDVM LCGPIPTPGV AYLTKALRLS AGVVISASHN PYQDNGIKFF
     SAKGDKLSDD FELAIEAELE NPIGCVSSKE LGKAFRLDDA AGRYIEFCKS TFPGDLNLKG
     LKLVVDCANG AAYHTAPHVF HELGAEVISI GVSPDGRNIN DGCGATAPAA LIAKVKEEGA
     DLGIALDGDA DRLQMVDSTG RLFNGDELLY VLAKDRIDRG QQLGGVIGTL MTNLAIENAI
     KGLGIGFERA NVGDRYVLEL LKQKGWLIGG EGSGHLLCLD QHSTGDGTIA ALQVLAAMSQ
     NKKSLSELLN TVKIFPQVLL NVKLKPSYDW KSDEVLNKQI TKVEADLKDA GRVLIRASGT
     EPLLRVMVET QSADVAMNAA KSIADLVPTP
//

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