ID A0A1X6WYB5_9MICO Unreviewed; 607 AA.
AC A0A1X6WYB5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:SLM90851.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:SLM90851.1};
GN ORFNames=FM110_05720 {ECO:0000313|EMBL:SLM90851.1};
OS Brachybacterium nesterenkovii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=47847 {ECO:0000313|EMBL:SLM90851.1, ECO:0000313|Proteomes:UP000195981};
RN [1] {ECO:0000313|EMBL:SLM90851.1, ECO:0000313|Proteomes:UP000195981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP104813 {ECO:0000313|EMBL:SLM90851.1,
RC ECO:0000313|Proteomes:UP000195981};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FWFG01000050; SLM90851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6WYB5; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000195981; Unassembled WGS sequence.
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; 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 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 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:SLM90851.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000195981}.
FT DOMAIN 86..206
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 258..356
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 370..471
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 547..569
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 62975 MW; D85ADBB476DDDEC0 CRC64;
MRPDGTTPDG TTPDGTTPDG TTPDAAAEGT GAQGLSAALR ETARAWLADD PDPRTAAQLG
ALLERADAGD SAALAELTDA FAGPLQFGTA GLRGAMGPGS NRMNLAVVSR AARGIADHLL
DLLGGAGTDQ APLVVIGHDA RHNSRAFAEA SAQIMTAAGL RVRLTDGFCP TPLIAYATRA
LDADAGIVVT ASHNPPADNG YKVYLGARAS EPDGRGVQIV PPSDAQIAAA IAAVGPVREI
PRAESGWEVL GADLREAYLD AICALPLPDA PREVRIVHTA MHGVGHDTAM AALTRAGFSE
IHSVAKQADP DPDFPTVAFP NPEEKGAIDL ALELARTVEA DVVIANDPDA DRCAAAVLDP
HLGDWRMLRG DELGVLLGHH LIAEHRYTGV MAASVVSSRW LGRIARDAGR ESATTLTGFK
WIARTPGIAF GYEEAIGYCV LPDVVRDKDG LSTALLVAEM AALAKSRGTS LVGMLDSLAR
EHGLHATDQL SVRVEDLSLI GQMMTRLRQS PPASLAGSEV TTVQDLAQGS VETTGLPPTD
GMLLACADDA RVIVRPSGTE PKLKAYIEVI EAVPAGADEA AMGAVRERAA EHLARIVADV
RSALGVA
//
