ID A0A1H0RED8_9MICO Unreviewed; 480 AA.
AC A0A1H0RED8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:SDP27549.1};
GN ORFNames=SAMN04489867_1925 {ECO:0000313|EMBL:SDP27549.1};
OS Pedococcus dokdonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Pedococcus.
OX NCBI_TaxID=443156 {ECO:0000313|EMBL:SDP27549.1, ECO:0000313|Proteomes:UP000199077};
RN [1] {ECO:0000313|Proteomes:UP000199077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22329 {ECO:0000313|Proteomes:UP000199077};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; LT629711; SDP27549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0RED8; -.
DR STRING; 443156.SAMN04489867_1925; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000199077; Chromosome i.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 11..126
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 164..269
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 278..390
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 395..477
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 480 AA; 50085 MW; D176B9FE466BAE81 CRC64;
MPKPVLSDFV KAYDVRGVVP DQLNVDVAWA LGAAFAQTVI GPEGASGVVI GHDMRPSSPE
LSRAFAAGVT AHGFDATLIG LCSTDGLYYA SGALDLPGAM FTASHNPAQY NGIKLCRAGA
RPVGQDSGLA DVSALAQRLL DTGTSAGPVD GPVGTVVERD VLADYAAFLR GLVDLSGVRP
LKVVVDAGNG MGGHTVPAVL GTAAGLPGLP LEVVPLYFEL DGTFPNHEAN PLEPENLRDL
QAAVVEHGAD LGLAFDGDAD RCFVVDERGE PVSPSAITAL VATREVAKEV AGGTPAADVA
VVYNVISSAA VPEIIAEQGA RGVRTRVGHS FIKAEMAREG AVFGGEHSAH YYFRDFWFAD
TGMLAAMHVL AALGEQAEPL SRLTAAYSRY AASGEINSTV ADAAATTATV RAWATERGAQ
LDELDGLTAT HPATPEAPMW WLNLRASNTE PLLRLNVEAA DRDTMTQVRD DVLALVRGER
//
