ID W5XZ97_9CORY Unreviewed; 519 AA.
AC W5XZ97;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:AHI21965.1};
GN ORFNames=B843_02870 {ECO:0000313|EMBL:AHI21965.1};
OS Corynebacterium vitaeruminis DSM 20294.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI21965.1, ECO:0000313|Proteomes:UP000019222};
RN [1] {ECO:0000313|EMBL:AHI21965.1, ECO:0000313|Proteomes:UP000019222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "The complete genome sequence of Corynebacterium vitaeruminis DSM 20294.";
RL Submitted (FEB-2013) 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; CP004353; AHI21965.1; -; Genomic_DNA.
DR AlphaFoldDB; W5XZ97; -.
DR STRING; 1224164.B843_02870; -.
DR KEGG; cvt:B843_02870; -.
DR PATRIC; fig|1224164.3.peg.568; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_2_11; -.
DR Proteomes; UP000019222; Chromosome.
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 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; 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:UP000019222}.
FT DOMAIN 40..144
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 184..272
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 286..392
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 519 AA; 55555 MW; 9C2FF2421F32DF49 CRC64;
MNVRQVTRIS AGVAAWLAEQ AAQSPHAVES VYPGDSAPSI GLAFHEDDAA LRIVVGYDAR
YGSHAFATAT AEVFAGAGFE VFLMPTTTPT PIVPWLIKQW HLDGGVQITA SHNPAPDNGY
KVYTSLGRQI SSAAASEIEG CIDAVGPAVD VPRVFVRPAS DQLRRYVDDV VGLVAPKQAD
LLRVNNERAS LRIAFTAMHG VGGRALMQGL QAAGFVHIFP VAEQHYPDPT FPTVEFPNPE
EPAAVERLLA HGEKVDADVL IALDPDADRC AVGVRCKDGT LRMLRGDETG PLLATRLIPR
WDGSDTGKRP IVASTIVSSQ LLPAIAADRG WDLRQTLTGF KNLMAAAGTE QIAYGCEEAV
GIAPAPALVD DKDGIATALL ICAWAAELKA RRLTLLDELD ELYRAYGVHV GHQISARTVN
PTALITSLSR VPWEELLGFP GEVRSLAEVS GLPAMNGMQF LGQHEAGRVR IIARASGTES
KAKIYIEITQ DPGDLSRRHE AAELLESVSR TVSALVARL
//
