ID A0A0A2EX62_9PORP Unreviewed; 475 AA.
AC A0A0A2EX62;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphoglucosamine mutase {ECO:0000313|EMBL:KGN82120.1};
GN ORFNames=HW49_02820 {ECO:0000313|EMBL:KGN82120.1};
OS Porphyromonadaceae bacterium COT-184 OH4590.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae.
OX NCBI_TaxID=1517682 {ECO:0000313|EMBL:KGN82120.1, ECO:0000313|Proteomes:UP000030107};
RN [1] {ECO:0000313|EMBL:KGN82120.1, ECO:0000313|Proteomes:UP000030107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-184 OH4590 {ECO:0000313|Proteomes:UP000030107};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonadaceae COT-184_OH4590 Genome sequencing.";
RL Submitted (AUG-2014) 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:KGN82120.1}.
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DR EMBL; JRAN01000012; KGN82120.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2EX62; -.
DR eggNOG; COG1109; Bacteria.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000030107; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
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};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000030107}.
FT DOMAIN 8..144
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 173..266
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 273..379
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 404..459
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 475 AA; 51384 MW; 21472507844D83F5 CRC64;
MTLIKSISGI RGTIGGKVSD NLTPFDIVKF VSAYAEWLKE TSNAVDNKKL KVVVGRDARL
SGLMVENLVC GTLVGCGIDV VNIGLATTPT TEISVTAEQA DGGIIITASH NPKQWNALKL
LDSKGEFLSK ANGETILAIA ERPDSKYAEV DDLGKISYKD MTQYHIDSVL ALELVDVEAI
RNANFSVVID CVNSVGGVVI PQLLKALGVN NVICLNCEPT GNFAHNPEPL KENLTEISSY
IAQNKVDVGF VVDPDVDRLA IVCEDGEMFG EEYTLVSVAD YVLSNTKGNT VSNLSSTRAL
ADVTVMHGGN YYAAAVGEVN VVEKMKEVGA VIGGEGNGGV IYPASHYGRD ALVGIALFLT
LLAKKAMKVS ELRAIYPNYF ISKNKIELTS KIDVDTILEV IKGNYKHYKI NDIDGVKIDF
PQGWVHLRKS NTEPIVRIYS EAPTEEQADK FACAIISEIE RIVGDMDGGL ERDLF
//
