ID Q117H1_TRIEI Unreviewed; 479 AA.
AC Q117H1;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:ABG50353.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:ABG50353.1};
GN OrderedLocusNames=Tery_0970 {ECO:0000313|EMBL:ABG50353.1};
OS Trichodesmium erythraeum (strain IMS101).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Trichodesmium.
OX NCBI_TaxID=203124 {ECO:0000313|EMBL:ABG50353.1};
RN [1] {ECO:0000313|EMBL:ABG50353.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMS101 {ECO:0000313|EMBL:ABG50353.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Richardson P.;
RT "Complete sequence of Trichodesmium erythraeum IMS101.";
RL Submitted (JUN-2006) 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}.
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DR EMBL; CP000393; ABG50353.1; -; Genomic_DNA.
DR AlphaFoldDB; Q117H1; -.
DR STRING; 203124.Tery_0970; -.
DR KEGG; ter:Tery_0970; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_3; -.
DR OrthoDB; 9806956at2; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05800; PGM_like2; 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 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 PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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:ABG50353.1};
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 5..144
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 161..268
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 276..381
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 415..468
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 479 AA; 52664 MW; F01B2B51DA5562BA CRC64;
MAKPIKFGTD GWRGVIADDF TFERVTLVAP IAAKILDKNY ADSTNNSKTI IVGHDRRFMA
EEFAQVAAEA IQNAGFDVLL TDTYAPTPAF SLAAFQKKAL GAIVMTASHN PGKYLGLKVK
GAFGGSVPPE ITKQIEDLLT VETEKNLVQE GKIETFNPWQ NYCETLKKMV EIHSIKSAIN
EGKLKVFADV MHGAAAGGLQ QILGVEIEEV NGNRDPFFDG GAPEPLPRYL SKLFKRIKSY
RAANEGSLAI GLVFDGDSDR IAAVDGEGNF LSSQILIPIL IEHLTTTHGC SGEVVKTISG
SDLFPKVAEL YKMPVFETPI GYKYIADRML STQVLVGGEE SGGIGYGTHI PERDALLSAL
YLLEAVVMSS EDLTTIYRHL QEKTGFSSVY DRIDLPLLNM GVRSRLLEEL INNPVTEVAG
QKVLDCITID GYKFRLADGR WLLIRFSGTE PVLRLYCEAT DMQKVKQTLE WAKNWANSI
//
