ID   B9DZU1_CLOK1            Unreviewed;       457 AA.
AC   B9DZU1;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Phosphomannomutase/phosphoglucomutase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=CKR_0715 {ECO:0000313|EMBL:BAH05766.1};
OS   Clostridium kluyveri (strain NBRC 12016).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=583346 {ECO:0000313|EMBL:BAH05766.1, ECO:0000313|Proteomes:UP000007969};
RN   [1] {ECO:0000313|Proteomes:UP000007969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12016 {ECO:0000313|Proteomes:UP000007969};
RA   Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K., Vertes A.A.,
RA   Yukawa H.;
RT   "Complete genome sequence of Clostridium kluyveri and comparative genomics
RT   of Clostridia species.";
RL   Submitted (SEP-2005) 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}.
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DR   EMBL; AP009049; BAH05766.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9DZU1; -.
DR   KEGG; ckr:CKR_0715; -.
DR   HOGENOM; CLU_016950_6_0_9; -.
DR   Proteomes; UP000007969; Chromosome.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd03089; PMM_PGM; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
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; IPR005841; Alpha-D-phosphohexomutase_SF.
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   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE   3: Inferred from homology;
FT   DOMAIN          3..98
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          131..227
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          233..346
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
SQ   SEQUENCE   457 AA;  51422 MW;  F7F6CA6C876489AC CRC64;
     MENNKIKIAI GIDSRLSGLE FKRCICEELL NLGCYVYDCG LCTTPAMFMT TVTGSYRCHG
     AIMITGSHLP YYYNGLKFFT ESGGCEKEDI KYILNRALNK YDNSVHSRGN IFKIDFIDEY
     SGILVKKIRE GINSKVNYNR PLSELKIIVD AGNGAGGFFA NKVLEPLGAK IEGSQFIIPD
     GKFPNHLPNP EDKEAMHSIK EAVIKNKADL GIIFDADVDR AAIVDCSGRE INRNALIALI
     STIVLEEYPG TTIVTDSVTS DGLSEFIQEL GGKHHRFKRG YRNVINEGIR LNNQNEGCYL
     AIETSGHAAF KENYFLDDGA YLIAKVLIKM ARLKSEGKSI EDLIQNMKMP VESLEFRFDI
     LDENFKEYGD KILEELKLYI EKVEGWSEVS PNYEGIRINC CSFKGSGWLL LRLSLHEPVL
     CLNIECDLSG YSNIIIDKLK SFLIEYKELD ITSLKTH
//