ID A6ETE7_9BACT Unreviewed; 572 AA.
AC A6ETE7;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:EDM43212.1};
GN ORFNames=SCB49_12074 {ECO:0000313|EMBL:EDM43212.1};
OS unidentified eubacterium SCB49.
OC Bacteria; Bacteroidota; environmental samples.
OX NCBI_TaxID=50743 {ECO:0000313|EMBL:EDM43212.1, ECO:0000313|Proteomes:UP000003659};
RN [1] {ECO:0000313|EMBL:EDM43212.1, ECO:0000313|Proteomes:UP000003659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCB49 {ECO:0000313|EMBL:EDM43212.1,
RC ECO:0000313|Proteomes:UP000003659};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM43212.1}.
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DR EMBL; ABCO01000010; EDM43212.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ETE7; -.
DR STRING; 50743.SCB49_12074; -.
DR Proteomes; UP000003659; 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:UP000003659}.
FT DOMAIN 48..185
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 222..315
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 333..437
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 572 AA; 63356 MW; 0565EEF3CB0065C1 CRC64;
MIHIDPSILD KVNTWLTPTF DKETQEEIKE MIAHDPEGLE DSFYKSLAFG TGGMRGVMGV
GDNRINKYTL GKNTQGISEY LKKQFPSETL KVAIAYDCRH NSKELAKVVA DVFSANGIHV
YLFTDLRPTP ELSFAVKHLE CHCGIVLTAS HNPPEYNGYK VYWQDGGQLV PPQDGEIIDL
INSLDYNDIN FKGDNTLIKA IDKEVDDAFA AASLKNGCKV KDNSLRENLK VVFTSLHGTS
ITMIPRVLED AGYTNVHLVK EQESPDGDFP TVVSPNPEEP EALSMAIALA DKEQADIVIG
TDPDCDRLGI AVRDSDGKMQ ILNGNQAMAI KTYFLLDQLK EQKALNQKHF IASTIVSTPM
IAKIAAKFGV MYKEGLTGFK WIAKMVKDFP ELDFVGGGEE SFGYMVGDFV RDKDAVTATL
LACEIAAIEK AKGNTLLDYF NTVQNEVGYY KEHLISVVKK GKKGAEEIAE ILKQLRENPF
TEINGSKVVR IEDYLTSESK DLVKNISETI EIPKSNVLIY YTEDGSKIAA RPSGTEPKIK
FYMSVTVQGG NTDTVLDQRI KDIQTSLNNL TS
//
