ID W0DWY5_9GAMM Unreviewed; 507 AA.
AC W0DWY5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AHF01499.1};
GN ORFNames=THIAE_06775 {ECO:0000313|EMBL:AHF01499.1};
OS Thiomicrospira aerophila AL3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Thiomicrospira.
OX NCBI_TaxID=717772 {ECO:0000313|EMBL:AHF01499.1, ECO:0000313|Proteomes:UP000005380};
RN [1] {ECO:0000313|EMBL:AHF01499.1, ECO:0000313|Proteomes:UP000005380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AL2 {ECO:0000313|Proteomes:UP000005380};
RG DOE Joint Genome Institute;
RA Kappler U., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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}.
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DR EMBL; CP007030; AHF01499.1; -; Genomic_DNA.
DR RefSeq; WP_006461032.1; NZ_CP007030.1.
DR AlphaFoldDB; W0DWY5; -.
DR STRING; 717772.THIAE_06775; -.
DR KEGG; tao:THIAE_06775; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_6_0_6; -.
DR InParanoid; W0DWY5; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000005380; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03089; PMM_PGM; 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; IPR005841; Alpha-D-phosphohexomutase_SF.
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 PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 10..146
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 179..280
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 285..387
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 507 AA; 55054 MW; 7FAC6EF8B078BC7C CRC64;
MEQASWVQLQ NGSDIRGVAL LGIADQPVNL TASHANSIGQ AFAQWLSAKL NKPAAELKVA
IGRDSRLSGP DLAQGLAEGL MATGVAVTDF GLASTPAMFM ATVKPALDQD VFDGSVMITA
SHLPFNRNGF KFFTDAGGLD KPDIHQLLRL AAQSPHQACE QPVNTLDYMS IYAADLVNKV
RQAINHPSDY HQPLKGLKII VDAGNGAGGF FVDKVLQPLG ADTQGSQFLA PDGHFPNHVP
NPEDAQAMQS ICAAVVHHQA DLGLIFDTDV DRSAAVDEHG QAINRNRLIA LMAAILLKDA
PGATIVTDSV TSDGLTDFIE HQLQGKHHRF KRGYKNVINE AIRLNNQGVL TPLAIETSGH
AALKDNYFLD DGAYLVTLLL IELAKAKLLN LSLTSLIATL QEPVEEQERR FHILQPDFQH
YGQQVLDALT HYVAKQPGWR QVPNNYEGIR VACQADDEQG WFLLRLSLHD PVLALNVESN
IAGGVDNILA RLMTFMAEFK QDLTLAS
//
