ID A0A0S2I495_9BACT Unreviewed; 462 AA.
AC A0A0S2I495;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0000313|EMBL:ALO17074.1};
DE EC=5.4.2.2 {ECO:0000313|EMBL:ALO17074.1};
GN Name=algC_2 {ECO:0000313|EMBL:ALO17074.1};
GN ORFNames=L21SP5_03463 {ECO:0000313|EMBL:ALO17074.1};
OS Salinivirga cyanobacteriivorans.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Salinivirgaceae;
OC Salinivirga.
OX NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO17074.1, ECO:0000313|Proteomes:UP000064893};
RN [1] {ECO:0000313|EMBL:ALO17074.1, ECO:0000313|Proteomes:UP000064893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO17074.1,
RC ECO:0000313|Proteomes:UP000064893};
RA Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT "Description and complete genome sequence of a novel strain predominating
RT in hypersaline microbial mats and representing a new family of the
RT Bacteriodetes phylum.";
RL Submitted (NOV-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}.
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DR EMBL; CP013118; ALO17074.1; -; Genomic_DNA.
DR RefSeq; WP_057954402.1; NZ_CP013118.1.
DR AlphaFoldDB; A0A0S2I495; -.
DR STRING; 1307839.L21SP5_03463; -.
DR KEGG; blq:L21SP5_03463; -.
DR PATRIC; fig|1307839.3.peg.3717; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000064893; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:InterPro.
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; 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 InterPro; IPR024086; GlmM_arc-type.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
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 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:ALO17074.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000064893}.
FT DOMAIN 8..140
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 168..263
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 270..374
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 395..456
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 462 AA; 50625 MW; 854E58EDC261892D CRC64;
MALIKSISGI RGTIGGRPGN NLTPVDIVKF VAAYGQWLKN QQEKNQYTVV VGRDARISGS
MVKMLVNATL SGLGINVLDI DLASTPTTEM AVTHFNADGG LILTASHNPR EWNALKMLNK
KGEFLNAAEG EAILTIADEN TIHYVDVDHL GTIQEARYHD EHIKAILDLE LVHKDAIAAK
NFKVVVDGIN SVGSLIIPDL LRALGVKEII ELNSEANGQF AHPAEPLPEN VVDICNTVKK
HKADLGIVVD PDVDRLALID EKGVMFGEEY TIVAVAEYVL HHNSGNAVSN LSSSRALRDI
TEQAGGNYFA SAVGEVNVVA TMKERNAVIG GEGNGGVIYP ELHYGRDALI GIALFLSHLA
KMNISVSKLK KRYPSYTIIK DKINLSSKLN LDRLLDEIAR IYRNENVNRT DGVKIDLDNG
WIHLRKSNTE PIIRIYCEAH TIKEAQQLAN KIKQEINRSI AN
//
