ID Q83H44_TROWT Unreviewed; 550 AA.
AC Q83H44;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:AAO44114.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:AAO44114.1};
GN Name=pmmB {ECO:0000313|EMBL:AAO44114.1};
GN OrderedLocusNames=TWT_017 {ECO:0000313|EMBL:AAO44114.1};
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Tropherymataceae;
OC Tropheryma.
OX NCBI_TaxID=203267 {ECO:0000313|EMBL:AAO44114.1, ECO:0000313|Proteomes:UP000002200};
RN [1] {ECO:0000313|EMBL:AAO44114.1, ECO:0000313|Proteomes:UP000002200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist {ECO:0000313|EMBL:AAO44114.1,
RC ECO:0000313|Proteomes:UP000002200};
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
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; AE014184; AAO44114.1; -; Genomic_DNA.
DR RefSeq; WP_011095990.1; NC_004572.3.
DR AlphaFoldDB; Q83H44; -.
DR STRING; 203267.TWT_017; -.
DR GeneID; 67387797; -.
DR KEGG; twh:TWT_017; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_0_2_11; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000002200; 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:AAO44114.1};
KW Magnesium {ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|RuleBase:RU004326};
KW Reference proteome {ECO:0000313|Proteomes:UP000002200}.
FT DOMAIN 48..185
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 207..313
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 318..426
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 550 AA; 60555 MW; E504CB41AEF5A514 CRC64;
MNILRKASLW IENDPVAITR LEMRRLLAES EKTGDVRELE ERLSKTLEFG TAGLRAPQGA
GFNRVNAVVT AQAANALSQF LLEENRGRTL VIGYDGRYNS QLWARNTARI ASSYDITALI
MPRALPTPLL AFAVRQLGAA AGVMVTASHN PREYNGYKVY LGGEDKGAQI PDTAAAKIAK
NLRDEVAYSD IPMKDSYGIL DEEIIEAYLS RTAKAIKRQF GSPKADLKIC HTAMHGVGHE
IFVRLMEKLG FHNLVFVEEQ KMPDPAFPTL PFPNPEEKGA LDLAFETARL AECDIIIAND
PDADRVAVAH PDGKVFTGNE IGALLGVEIA RMQRGHGVLS NSMVSSPIMR RIAETYGMQH
VETPTGFKWV ARVPDICFGF EEALGYMIHP ELVRDKDGLS AGAAIATIAA SQKAQGRSLR
DCLDDLQSKL GYFRSTQYAV RMASLDSVQA VMQNLRAESL NKIGRFRVTK YRDLLFGSPP
VDLLEFNLGQ DIDDLFGRLI VRPSGTELKL KCYIDSVAKT PDGAEQLLSE LTYACKNLLC
ETSRRGGAEN
//
