ID W0F0T6_9BACT Unreviewed; 575 AA.
AC W0F0T6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:AHF15064.1};
GN ORFNames=NIASO_07675 {ECO:0000313|EMBL:AHF15064.1};
OS Niabella soli DSM 19437.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niabella.
OX NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF15064.1, ECO:0000313|Proteomes:UP000003586};
RN [1] {ECO:0000313|EMBL:AHF15064.1, ECO:0000313|Proteomes:UP000003586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG DOE Joint Genome Institute;
RA Eisen J., 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 -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC {ECO:0000256|ARBA:ARBA00010231}.
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DR EMBL; CP007035; AHF15064.1; -; Genomic_DNA.
DR RefSeq; WP_008584871.1; NZ_CP007035.1.
DR AlphaFoldDB; W0F0T6; -.
DR STRING; 929713.NIASO_07675; -.
DR KEGG; nso:NIASO_07675; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_0_10; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000003586; 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; cd05799; PGM2; 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; IPR036900; A-D-PHexomutase_C_sf.
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 PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000003586}.
FT DOMAIN 45..183
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 206..309
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 321..442
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 575 AA; 64019 MW; DF38A81EBB9144E9 CRC64;
MDSAIQQKVD QWLQGNYDPE TKDTIKQLEK NDPKQLEDAF YQNLEFGTGG LRGIMGVGTN
RMNKYTVGMA TQGYANYLIQ SFPGTEVRVA IAHDSRNNSR FFAETTAHVF AANGIKVFLF
EALRPTPELS FAIRTLKCQG GVVCTASHNP KEYNGYKAYW NDGGQLVPPH DKNVIKEVEK
IASVDDVKWT GQDENITIIG KDIDEQYIEM VKGLSVFPEV IEKQSDLKIV YTPIHGTGIT
LVPLVLERFG FKNVTIVEEQ KTPDGNFPTV EYPNPEEKET MSIGLQKAKA LDADILLGTD
PDADRVGIGV KNNHGEWVLM NGNQTAVLAF NYLLEARKEK GIAQANDMII TTIVTTGMAD
ELAKGYGVNC YRVLTGFKWI AELIREKEGK ETYIIGGEES FGLMIGDKIR DKDAVSAVAL
LCEMAAYEKN KGKTLFDKLI ELYIKFGFYK EKLISITKKG MDGQQQIAAM MQQYRDNLPK
EINGSKVVRV LDYQSSKSTD PHTGEATDIL LPKSNVLQFR LEDGSLISAR PSGTEPKIKF
YFSVREQLSS GAEFDATDKK LDAKIDGIIA AMQLQ
//