ID A0A0G3GU92_9CORY Unreviewed; 527 AA.
AC A0A0G3GU92;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:AKK02442.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:AKK02442.1};
GN Name=pmmB {ECO:0000313|EMBL:AKK02442.1};
GN ORFNames=CEPID_02810 {ECO:0000313|EMBL:AKK02442.1};
OS Corynebacterium epidermidicanis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK02442.1, ECO:0000313|Proteomes:UP000035368};
RN [1] {ECO:0000313|EMBL:AKK02442.1, ECO:0000313|Proteomes:UP000035368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK02442.1,
RC ECO:0000313|Proteomes:UP000035368};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium epidermidicanis DSM 45586,
RT isolated from the skin of a dog suffering from pruritus.";
RL Submitted (MAY-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; CP011541; AKK02442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3GU92; -.
DR STRING; 1050174.CEPID_02810; -.
DR KEGG; cei:CEPID_02810; -.
DR PATRIC; fig|1050174.4.peg.570; -.
DR Proteomes; UP000035368; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
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 Isomerase {ECO:0000313|EMBL:AKK02442.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000035368}.
FT DOMAIN 17..168
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 188..294
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 308..418
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 527 AA; 56386 MW; 3EEE35CD0A33CE6F CRC64;
MRFGTTFEGM SLPRELNFGT AGMRAPIGPA TDQMNVTQVT RVTAGVAAWL AHKIGQERNE
HPVASVCSQQ GPLRVVVGYD ARYGSPNFAI TAAEVFAGAG FEVTLLPAPA PTQIIPWLIR
FRGLDAGVQI TASHNPSAYN GYKVYLADGA QLDASAEREI EAMIREVTSP IDVPRVMVRP
TTDQLRRYID DITDLIAPTQ AELLRVNNER AALKVAYTSL HGVGGRAMTQ ALQAAGFAQI
FPVLAQHYPD PLFPTVDFPN PEEPGVTDLL LGTAAEHDVD VLIALDPDAD RCAIGVRTAD
GSHRMLRGDE LGPLLATRLV PPFLGGGPAP VVVTSEVSSR LLQVIAAERG WDYQESCTGF
KNLIRAATSR PGELVFAYEE ANGTAPAPHL VADKDGIATA LFACAWAAEL KAQGLTLLDE
LTALHKRYGI FAGTQVAVRT SDPEGLLAAL RAHPPTHLAG ETIHAADLSI SDGILLSGAG
VRALARTSGT ENKLKFYLEV HQPWTPEGAN EQLERLRAEV ELLVASL
//
