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Database: UniProt
Entry: A0A3E1F0L5_9FLAO
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ID   A0A3E1F0L5_9FLAO        Unreviewed;       461 AA.
AC   A0A3E1F0L5;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:RFC55257.1};
DE            EC=5.4.2.10 {ECO:0000313|EMBL:RFC55257.1};
GN   Name=glmM {ECO:0000313|EMBL:RFC55257.1};
GN   ORFNames=DXU93_05400 {ECO:0000313|EMBL:RFC55257.1};
OS   Brumimicrobium aurantiacum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Crocinitomicaceae; Brumimicrobium.
OX   NCBI_TaxID=1737063 {ECO:0000313|EMBL:RFC55257.1, ECO:0000313|Proteomes:UP000257127};
RN   [1] {ECO:0000313|EMBL:RFC55257.1, ECO:0000313|Proteomes:UP000257127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N62 {ECO:0000313|EMBL:RFC55257.1,
RC   ECO:0000313|Proteomes:UP000257127};
RA   Du Z.-J., Luo H.-R.;
RT   "The draft genome squence of Brumimicrobium sp. N62.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231, ECO:0000256|RuleBase:RU004326}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RFC55257.1}.
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DR   EMBL; QURB01000002; RFC55257.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E1F0L5; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000257127; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   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; IPR024086; GlmM_arc-type.
DR   NCBIfam; TIGR03990; Arch_GlmM; 1.
DR   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 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:0000313|EMBL:RFC55257.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004326};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          8..142
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          164..264
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          271..377
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          394..457
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   461 AA;  49974 MW;  2ED6D6EBE3308B05 CRC64;
     MTLIKSISGI RGTIGGKVGE GLSPLDVVKF ASAYGTWLQQ ESNAKKLTIV IGRDARISGS
     IVNNLVISSL RSLGINVIDL GLSTTPTVEM AVTMEKAHGG IIITASHNPK QWNALKLLNG
     AGEFISGEEG EKVLKIAEEE SFDFAEVDHL GKLTENNDYI QKHIEAVLNL PYVDIEAIKK
     ADFSIVVDAV NSTGGIAVPL LLDALGVKKV TGIHCEPTGI FAHNPEPLPA HLTDLSEAIV
     EQKADLGITV DPDVDRLAMV CEDGTMFGEE YTLVAVADFV LAQKGGATVS NLSSTRALRD
     VTEKHGHDYY ASAVGEVNVV EKMKAVNAVI GGEGNGGVIL PELHYGRDAL VGIALFLTHL
     ANKKMKVTEL RDSYPKYIIS KNKLQLTPET NVDKVLVEMA DKYSKQEVDS TDGVKIYFEK
     EWVHLRKSNT EPIIRIYAES TDNTKADQLA KDIMQEIETI I
//
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