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Database: UniProt
Entry: A0A068R7N5_9GAMM
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ID   A0A068R7N5_9GAMM        Unreviewed;       445 AA.
AC   A0A068R7N5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Phosphoglucosamine mutase {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327};
DE            EC=5.4.2.10 {ECO:0000256|HAMAP-Rule:MF_01554, ECO:0000256|RuleBase:RU004327};
GN   Name=glmM {ECO:0000256|HAMAP-Rule:MF_01554,
GN   ECO:0000313|EMBL:CDG23029.1};
GN   ORFNames=XPG1_3393 {ECO:0000313|EMBL:CDG23029.1};
OS   Xenorhabdus poinarii G6.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=1354304 {ECO:0000313|EMBL:CDG23029.1, ECO:0000313|Proteomes:UP000032735};
RN   [1] {ECO:0000313|EMBL:CDG23029.1, ECO:0000313|Proteomes:UP000032735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G6 {ECO:0000313|EMBL:CDG23029.1,
RC   ECO:0000313|Proteomes:UP000032735};
RA   Genoscope - CEA;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:0000256|HAMAP-Rule:MF_01554,
CC         ECO:0000256|RuleBase:RU004327};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01554};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01554};
CC   -!- PTM: Activated by phosphorylation. {ECO:0000256|HAMAP-Rule:MF_01554}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|HAMAP-Rule:MF_01554,
CC       ECO:0000256|RuleBase:RU004326}.
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DR   EMBL; FO704551; CDG23029.1; -; Genomic_DNA.
DR   RefSeq; WP_045959945.1; NZ_FO704551.1.
DR   AlphaFoldDB; A0A068R7N5; -.
DR   STRING; 1354304.XPG1_3393; -.
DR   KEGG; xpo:XPG1_3393; -.
DR   HOGENOM; CLU_016950_7_0_6; -.
DR   OrthoDB; 9803322at2; -.
DR   Proteomes; UP000032735; 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   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 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   NCBIfam; TIGR01455; glmM; 1.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOSAMINE MUTASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 1.
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; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01554};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01554};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01554};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_01554}.
FT   DOMAIN          4..135
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          157..254
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          258..365
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          373..442
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
FT   ACT_SITE        102
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         102
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01554"
SQ   SEQUENCE   445 AA;  47920 MW;  CFE6A60D8486167D CRC64;
     MSNRKYFGTD GIRGKVGNTP ITPDFVLKLG WAAGKVLARH GSRKIIIGKD TRISGYMLES
     ALEAGLAAAG LSASFTGPMP TPAVAYLTRT FRAEAGIVIS ASHNPYYDNG IKFFSIDGTK
     LPDDVEEAIE AEMEKPLTCV ESAELGRANR IVDAAGRYIE FCKGTFPSEQ SLNGLKIVLD
     CANGATYHIA PNVLRELGAE VITVGCEPNG ININEECGAT DVSLLQRRVL EEQAHVGLAF
     DGDGDRIIMV DHLGQKVDGD QILYIIAREA LRQGQLRGGA VGTLMSNMGL ELALKQLGIP
     FERAKVGDRY VLEKLQEKGW RLGAENSGHV ILLDKTTTGD GIVAGLQVLS AMVRNTMSLH
     DLCSGMKLLP QILVNVRFTG DHDPLQAESV QEAVKSVESE LEGCGRVLLR KSGTEPLIRV
     MVEGEDKDQV TALAHRIADA VKKIG
//
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