(data stored in SCRATCH zone)

SWISSPROT: C8W670_DESAS

ID   C8W670_DESAS            Unreviewed;       451 AA.
AC   C8W670;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
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=Dtox_0605 {ECO:0000313|EMBL:ACV61525.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61525.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61525.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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; CP001720; ACV61525.1; -; Genomic_DNA.
DR   RefSeq; WP_015756244.1; NC_013216.1.
DR   STRING; 485916.Dtox_0605; -.
DR   EnsemblBacteria; ACV61525; ACV61525; Dtox_0605.
DR   KEGG; dae:Dtox_0605; -.
DR   eggNOG; ENOG4107QJF; Bacteria.
DR   eggNOG; COG1109; LUCA.
DR   HOGENOM; HOG000268678; -.
DR   KO; K03431; -.
DR   OMA; MFGEEYT; -.
DR   OrthoDB; 1265792at2; -.
DR   BioCyc; DACE485916:G1GFV-611-MONOMER; -.
DR   Proteomes; UP000002217; 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; C8W670.
DR   SWISS-2DPAGE; C8W670.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01554,
KW   ECO:0000256|RuleBase:RU004327, ECO:0000256|SAAS:SAAS01085081,
KW   ECO:0000313|EMBL:ACV61525.1};
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:UP000002217}.
FT   DOMAIN        4    132       PGM_PMM_I. {ECO:0000259|Pfam:PF02878}.
FT   DOMAIN      159    254       PGM_PMM_II. {ECO:0000259|Pfam:PF02879}.
FT   DOMAIN      258    367       PGM_PMM_III. {ECO:0000259|Pfam:PF02880}.
FT   DOMAIN      376    443       PGM_PMM_IV. {ECO:0000259|Pfam:PF00408}.
FT   ACT_SITE    101    101       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01554}.
FT   METAL       101    101       Magnesium; via phosphate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01554}.
FT   METAL       241    241       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
FT   METAL       243    243       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
FT   METAL       245    245       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
FT   MOD_RES     101    101       Phosphoserine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
SQ   SEQUENCE   451 AA;  48437 MW;  2EA404DD43CF611F CRC64;
     MGVMFGTDGV RGVANRELTP ELAFKLGRAG AYILCKDNCN DRRIIIGKDT RISGDMLEAA
     LAAGICSVGV NVLKVGILPT PAIAYLTRSL GAAAGVVISA SHNPVEDNGI KFFGPTGYKL
     PDETEDSIET AVLGDFAGIP SPTGSALGRT YELKDALDRY IMFLQDTMDV DLTGLKVVVD
     CANGAAYKVA PRVLKELGAE VIPIFNRPDG VNINAWCGST YPVALQESVV ATGADIGLAH
     DGDADRLIAV DHEGNIVDGD RIMLTIAKYM KENDKLTRNT VVVTVMSNLG LHLALQKAGI
     KVVQTKVGDR YVMEKMLKLG ARFGGEQSGH IIFLKHNTTG DGVLTALQLM RVMKKTGRSL
     KALGEQMERL PQLLENVRVA DKAAIMNSPE LSAAIEKYEE QLAGQGRILV RPSGTEPLVR
     VMVEGRDKKE LEQISAAMIK LIHELSQGGD R
//

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