ID   A5CPM8_CLAM3            Unreviewed;       567 AA.
AC   A5CPM8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   04-NOV-2026, entry version 101.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:CAN01027.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:CAN01027.1};
GN   Name=manB {ECO:0000313|EMBL:CAN01027.1};
GN   OrderedLocusNames=CMM_0988 {ECO:0000313|EMBL:CAN01027.1};
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN01027.1, ECO:0000313|Proteomes:UP000001564};
RN   [1] {ECO:0000313|EMBL:CAN01027.1, ECO:0000313|Proteomes:UP000001564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN01027.1,
RC   ECO:0000313|Proteomes:UP000001564};
RX   PubMed=18192381; DOI=10.1128/JB.01595-07;
RA   Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M.,
RA   Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C.,
RA   Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(2008).
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; AM711867; CAN01027.1; -; Genomic_DNA.
DR   RefSeq; WP_012037674.1; NC_009480.1.
DR   AlphaFoldDB; A5CPM8; -.
DR   KEGG; cmi:CMM_0988; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_0_2_11; -.
DR   OMA; AAAWYKR; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000001564; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008973; F:phosphopentomutase activity; IEA:TreeGrafter.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:TreeGrafter.
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; 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   PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2B-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   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:CAN01027.1};
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:UP000001564}.
FT   DOMAIN          63..201
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          226..326
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          337..443
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          476..549
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   567 AA;  60634 MW;  B82BA9F08CD7FFA3 CRC64;
     MSREETAALV AAARAWQAQD PDPVTRAEVD ELLALVDGTA AGASAADREQ AAGGIRDRFQ
     TRLQFGTAGL RGELGAGPNR MNRVLVSQAA AGFADYLRSR SPRPSIVIGY DGRHNSRVFA
     EDTARIMAGA GVRTVLLPRA LPTPVLAYAV KHLAVSAGVM VTASHNPARD NGYKVYLGDE
     DHGAQIVSPA DRDIAAFIHK AAGERTVQQL PVADDYEIAP ETLIDSYVEE TAELFAAPLA
     PLRWVYTPLH GVGWETAARV FDAVGVDAPV VVAAQADPDP DFPTVDFPNP EEPGALDLAF
     EAAVRSDAEL IIANDPDADR LAVAIADEHG AWRRLSGNEV GMLLGLGIAE RYAADGNTGT
     FASSLVSSPA LEVVARELGF GYRETLTGFK WISRVPDLVY GYEEALGYLV APWITSDKDG
     ISAAVAVLHG VMLLKSRGQT IDDYDREFAE RFGSFASDQI SVRVTDLAVI PRIMAKLRQS
     PPTSIGSRRV ERMDDLAEGT ADLPPSDVLR FHLGDGARLI VRPSGTEPKI KVYLDAQSTE
     GTVAERRDAA RAVVADLAQA VPLLLEV
//