ID M1PR95_DESSD Unreviewed; 578 AA.
AC M1PR95;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:AGF78896.1};
GN OrderedLocusNames=UWK_02356 {ECO:0000313|EMBL:AGF78896.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF78896.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
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; CP003985; AGF78896.1; -; Genomic_DNA.
DR AlphaFoldDB; M1PR95; -.
DR STRING; 1167006.UWK_02356; -.
DR KEGG; dsf:UWK_02356; -.
DR PATRIC; fig|1167006.5.peg.2558; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_7; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000011721; 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 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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004326};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004326};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000011721}.
FT DOMAIN 70..216
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 277..359
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 367..474
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 522..569
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 578 AA; 62854 MW; 24B96301471AAB09 CRC64;
MSQAAKIKEL YKKCNIGKDH SESDYFGLVK ELVALRKAEG VQWQQAIDQV YALIMDEIIC
NAGEPVTAVK FGTSGWRGMI GKDLFVRSVS FVTAAIVDLY VALDEEPELG LFLGVTSLDE
ARKRGCVLGF DNRFGGEILA GAVTEVLVKA GFVVHYAGES TTGVLSAAVL ELNAAFSVNL
TPSHNPLEYA GFKYNAADAG PAATELTGRI TEKARQIIAG AGSPFVALDK PVVSAADRDD
VLPFDALGTW KQLVRNNKDI HDVHYDDIMN RFATDTEIVA VIDSVHGASR IHIPALFEGV
ENDRLIQLRD SSDVTFDGIA PEPSSANMVG VITTLQKRKE PLKVGAIIDP DGDRIRFTDG
TVEISMNQFG AMAYHFLHEG KGKKGMVAKT VATSNLANRL AEVFGEETFE PRVGFKEFKP
VIGKALVYFE ESDGISIIGH TPEKDAYIGL LLALDMVISR RQNLGEYLAE IEKEYGAFYP
DRDGLPVSVQ GEVLHAALLK LEKYGVGAVV NVGGTEQRIT QVIDIDGRKM IFEDGSWLMI
RPSGTEPKVR FYVESRTKSG TAALVEAARG MLDEIGLI
//
