(data stored in ACNUC7421 zone)

SWISSPROT: D6ZB73_SEGRD

ID   D6ZB73_SEGRD            Unreviewed;       453 AA.
AC   D6ZB73;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 54.
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=Srot_0345 {ECO:0000313|EMBL:ADG96832.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96832.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96832.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG96832.1; -; Genomic_DNA.
DR   RefSeq; WP_013137288.1; NC_014168.1.
DR   STRING; 640132.Srot_0345; -.
DR   EnsemblBacteria; ADG96832; ADG96832; Srot_0345.
DR   KEGG; srt:Srot_0345; -.
DR   eggNOG; ENOG4107QJF; Bacteria.
DR   eggNOG; COG1109; LUCA.
DR   HOGENOM; HOG000268678; -.
DR   KO; K03431; -.
DR   OMA; MFGEEYT; -.
DR   OrthoDB; 1265792at2; -.
DR   BioCyc; SROT640132:G1GLH-346-MONOMER; -.
DR   Proteomes; UP000002247; 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; D6ZB73.
DR   SWISS-2DPAGE; D6ZB73.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01554,
KW   ECO:0000256|RuleBase:RU004327, ECO:0000256|SAAS:SAAS01085081,
KW   ECO:0000313|EMBL:ADG96832.1};
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:UP000002247}.
FT   DOMAIN        4    131       PGM_PMM_I. {ECO:0000259|Pfam:PF02878}.
FT   DOMAIN      174    259       PGM_PMM_II. {ECO:0000259|Pfam:PF02879}.
FT   DOMAIN      263    373       PGM_PMM_III. {ECO:0000259|Pfam:PF02880}.
FT   DOMAIN      379    447       PGM_PMM_IV. {ECO:0000259|Pfam:PF00408}.
FT   ACT_SITE     98     98       Phosphoserine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01554}.
FT   METAL        98     98       Magnesium; via phosphate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01554}.
FT   METAL       246    246       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
FT   METAL       248    248       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
FT   METAL       250    250       Magnesium. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
FT   MOD_RES      98     98       Phosphoserine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01554}.
SQ   SEQUENCE   453 AA;  46520 MW;  BD572FAF4F534E1B CRC64;
     MTALFGTDGV RGVANTELTP ELALTLGSLA GSRLRGESGL AVVGRDPRIS GAMLEACVCA
     GLASSGVRVL RAGVLPTPAV SWLVKDLGAD LGVVVSASHN PMPDNGLKFF GPGGGKLDAE
     TENLLAADVS RVSKGGKASW GWGEGERPTG AGVGDLVDFP EGAARYVSRF APITPKAGQL
     RVVVDCANGA TSRLAAQVYE ATGAEVITLN AEPDGLNIND RCGSTHLDGL RAAVLEEGAD
     LGLAHDGDGD RCLAVAEDGD VVDGDAIMAV LALGLHERGQ LRHNKLVVTV MSNLGLHIAM
     RAAGVELEVT QVGDRHVTDA LREGGYSIGG EQSGHVVIPE LGETGDGMVT GLRLISRIVE
     SGKSLSELAS VVQVYPQVLV NVPVVDKLAA ASDLSVLDAV ASAQERLGGK GRVLLRPSGT
     EQLVRVMVEA ESALSAHEVA EQVAGLVRAT NLK
//

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