(data stored in ACNUC29543 zone)

HOGENOM: MARMS_1_PE1010

ID   MARMS_1_PE1010                       STANDARD;      PRT;   448 AA.
AC   MARMS_1_PE1010; A6VU24;
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; (MARMS_1.PE1010).
GN   Name=glmM; OrderedLocusNames=Mmwyl1_1022;
OS   MARINOMONAS SP. MWYL1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Marinomonas.
OX   NCBI_TaxID=400668;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MARMS_1.PE1010.
CC       Marinomonas sp. MWYL1 chromosome, complete genome.
CC       Genomes
CC   -!- ANNOTATIONS ORIGIN:GLMM_MARMS
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   -!- GENE_FAMILY: HOG000268678 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A6VU24; -.
DR   EMBL; CP000749; ABR69953.1; -; Genomic_DNA.
DR   RefSeq; YP_001339888.1; NC_009654.1.
DR   ProteinModelPortal; A6VU24; -.
DR   STRING; A6VU24; -.
DR   GeneID; 5366776; -.
DR   GenomeReviews; CP000749_GR; Mmwyl1_1022.
DR   KEGG; mmw:Mmwyl1_1022; -.
DR   eggNOG; COG1109; -.
DR   OMA; GVGSTHL; -.
DR   BioCyc; MSP400668:MMWYL1_1022-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; MARMS_1.PE1010; -.
KW   phosphoglucosamine mutase;
KW   Complete proteome; Isomerase; Magnesium; Metal-binding;
KW   Phosphoprotein.
SQ   SEQUENCE   448 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRKYFGTDGI RGKVGTTPIT PEFMLKLGWA AGQVFKENDK KILIGKDTRI SGYMFESALE
     SGIVAAGADV RLVGPMPTPA IAYLTRTFRA SAGIVISASH NPYTDNGIKF FSAEGGKISD
     ELEERIEYFL EQPMEVVESS QIGRAKRIDD AAGRYIEYCK GTFPIGLQLS GLKIVVDCAD
     GATYHVAPRV FSELGAEVIS IGVNPDGLNI NEFSGATKPE LLRKNVLAEE ADLGIALDGD
     GDRLILVDRH GVVRDGDDIL YIIANHLMRT GRFSGGVVGT LMSNFGLELA FSETGIGFSR
     AAVGDRYVNE KLMQHGWVLG GEPSGHIVCR SITTTGDGII AALQVLRAMV EEGKALDELL
     VGLVKFPQKL KNIRVAKRFV PNEEPTLQKA IAVANERLNG LGRVLLRASG TEPLIRVMVE
     GRDNDTVDEL VEYLVEEVNS VVSAKADT
//

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