ID A0A150AK43_9BACT Unreviewed; 574 AA.
AC A0A150AK43;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KXX70269.1};
GN ORFNames=AVL50_11730 {ECO:0000313|EMBL:KXX70269.1};
OS Flammeovirga sp. SJP92.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae;
OC Flammeovirga.
OX NCBI_TaxID=1775430 {ECO:0000313|EMBL:KXX70269.1, ECO:0000313|Proteomes:UP000075267};
RN [1] {ECO:0000313|EMBL:KXX70269.1, ECO:0000313|Proteomes:UP000075267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJP92 {ECO:0000313|EMBL:KXX70269.1,
RC ECO:0000313|Proteomes:UP000075267};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) 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:KXX70269.1}.
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DR EMBL; LQAQ01000060; KXX70269.1; -; Genomic_DNA.
DR RefSeq; WP_062616792.1; NZ_LQAQ01000060.1.
DR AlphaFoldDB; A0A150AK43; -.
DR STRING; 1775430.AVL50_11730; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000075267; Unassembled WGS sequence.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; 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 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 Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000075267}.
FT DOMAIN 45..182
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 205..311
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 320..437
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 574 AA; 63283 MW; 41A32AE9A6913A65 CRC64;
MDQIINQNVQ AWLEGPFDEA TKTEIKRLQA EDEQELKESF YKSLEFGTGG LRGIMGVGTN
RMNKYTVGMA TQGLANYVKQ QVEGTPKAAI AYDCRNNSSF FAEVAANVLA ANGFTVYLFD
ELRATPELSF AIRELGCHTG IVLTASHNPK EYNGFKAYWA DGGQVVPPHD GNIVAEVRKI
ESIEDVKWEG GAGEVVKINK EVDEPYLNML EGLAVSPEAI KAQKDLKIVF TSIHGTGITM
VPRILERLGF DNVHIIEEQA VVDGNFPTVV YPNPEEAEAL SMALAKAKEI DADILLGTDP
DADRVGIAIK NHKGEWTLLN GNQTAALLFN YVISARKKEG KAQDNDFVCK TIVTTDLIDR
FAKANGMPCY NVLTGFKYIA EVIKEKEGKE NFIVGGEESY GYLIGDSVRD KDAIAASSMI
CEMAAYYKNE GKSMFDQLID IYVEHGYFKE KLISITKKGM SGAEEIANMM KELRANPPAT
INGSTVLEMR DYQSSVATDL VSKEECTIDL PKSNVLQFFL EDGTKISARP SGTEPKIKFY
FSVNTSIASA DEFDAADAVL EERVAKIIED MKLK
//
