ID F9Y7D8_KETVW Unreviewed; 551 AA.
AC F9Y7D8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN Name=pgm {ECO:0000313|EMBL:AEM41066.1};
GN OrderedLocusNames=KVU_1227 {ECO:0000313|EMBL:AEM41066.1};
OS Ketogulonicigenium vulgare (strain WSH-001).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ketogulonicigenium.
OX NCBI_TaxID=759362 {ECO:0000313|EMBL:AEM41066.1, ECO:0000313|Proteomes:UP000000692};
RN [1] {ECO:0000313|EMBL:AEM41066.1, ECO:0000313|Proteomes:UP000000692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSH-001 {ECO:0000313|EMBL:AEM41066.1,
RC ECO:0000313|Proteomes:UP000000692};
RX PubMed=21994934; DOI=10.1128/JB.06007-11;
RA Liu L., Li Y., Zhang J., Zhou Z., Liu J., Li X., Zhou J., Du G., Wang L.,
RA Chen J.;
RT "Complete genome sequence of the industrial strain Ketogulonicigenium
RT vulgare WSH-001.";
RL J. Bacteriol. 193:6108-6109(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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; CP002018; AEM41066.1; -; Genomic_DNA.
DR RefSeq; YP_005795062.1; NC_017384.1.
DR AlphaFoldDB; F9Y7D8; -.
DR KEGG; kvl:KVU_1227; -.
DR PATRIC; fig|759362.5.peg.1263; -.
DR eggNOG; COG0033; Bacteria.
DR HOGENOM; CLU_009330_0_1_5; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000000692; Chromosome.
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 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; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 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; 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:0000313|EMBL:AEM41066.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000692}.
FT DOMAIN 22..161
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 193..294
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 304..415
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 551 AA; 58450 MW; 2668ECC7A31EE345 CRC64;
MGIDGTPKLA ITTQITSPIT GQKPGTSGLR KQTTVFMQPH YLENYVQAIF DGIGGVQGKT
LVLGGDGRFF NDTASATILR MAAANGAKHV IVGRNALLST PAASHLIRKN GADGGLILSA
SHNPGGEDGD FGLKFNSANG GPAAESITDA IYEASKTISQ YLISDQPAPA LDTDGTYMLD
GMVVEVIDPV TDYAALMETL FDFNAIRSLF ASGFRIKFDA MHAATGPYAR EIFVNRLGAT
GDSVINDTPL PDFGGGHPDP NPIWASELVA IMSAPDAPDF GAASDGDGDR NMIMGRGLYV
SPSDSLALLA AQMHLAPAYK DGLKGIARSM PTSAAADRVA VAKGVCSFET PTGWKFFGNL
LDSDMVSICG EESAGTGSNH VREKDGLWAV LLWLNILAVS GKSVTALMQD HWATYGRDYY
TRHDYENIET ERANAVFNGL RDRLADLPGQ TFGGLKVERA DEFNYDDPVD QSHSAQQGLR
VFFNDGARAV LRLSGTGTVG ATLRLYLEQP EPNLQRQAED PQAALARVIA AAGEVTQIAA
LTGRDAPDVI S
//
