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Database: UniProt/TrEMBL
Entry: A0A0H3AAH8_DESVV
LinkDB: A0A0H3AAH8_DESVV
Original site: A0A0H3AAH8_DESVV 
ID   A0A0H3AAH8_DESVV        Unreviewed;       453 AA.
AC   A0A0H3AAH8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:ABM29294.1};
DE            EC=5.4.2.8 {ECO:0000313|EMBL:ABM29294.1};
GN   OrderedLocusNames=Dvul_2278 {ECO:0000313|EMBL:ABM29294.1};
OS   Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=391774 {ECO:0000313|EMBL:ABM29294.1, ECO:0000313|Proteomes:UP000009173};
RN   [1] {ECO:0000313|Proteomes:UP000009173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DP4 {ECO:0000313|Proteomes:UP000009173};
RX   PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA   Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA   He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA   Stahl D.A.;
RT   "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT   plasticity.";
RL   Environ. Microbiol. 11:2244-2252(2009).
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; CP000527; ABM29294.1; -; Genomic_DNA.
DR   RefSeq; WP_011792758.1; NC_008751.1.
DR   AlphaFoldDB; A0A0H3AAH8; -.
DR   KEGG; dvl:Dvul_2278; -.
DR   HOGENOM; CLU_016950_9_1_7; -.
DR   OMA; KCSQVMY; -.
DR   Proteomes; UP000009173; 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; 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; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR43771:SF2; PHOSPHOMANNOMUTASE/PHOSPHOGLUCOMUTASE; 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:ABM29294.1};
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}.
FT   DOMAIN          8..138
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          153..250
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          254..358
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          372..443
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   453 AA;  49723 MW;  2E63AB5B0015E8B1 CRC64;
     MKALSAHVFR AYDIRGIVDT DFDPEWVERL GRACGTYFVS HGHGAAVVGF DCRHSSPAYH
     DALVRGLLST GVDVTSVGMV PTPVLYFAVK HLGRKAGVMI TASHNPSEYN GFKVVAGEST
     IHGEEIRRIW EIFERGEFAS GHGIGCSHDI VPSYIEAITS DVHPARKLKV VVDGGNGAGG
     ELCVEVLRRL GVEVVAQFCE PDGDFPNHHP DPVVEANMTA LMERVQVERA DLGIGLDGDA
     DRLGAVDGRG RLLNGDELLS LYAREMLARR PGETVIADVK CSHRLFDDIE AHGGKPMMWI
     TGHSVVKARM LEVGAPLAGE LSGHMFFGDR WFGFDDAIYG AARLVELLAA SDVPLTDLPG
     WPPSHATREL HLPCPEHAKF EVVRRAQAYF RERCTINDID GARVIFPDGW GLVRASNTQP
     VLVLRFEAQT PERLAEIRAF VEEPLRRWVA ELS
//
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