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Database: UniProt/TrEMBL
Entry: B1I307_DESAP
LinkDB: B1I307_DESAP
Original site: B1I307_DESAP 
ID   B1I307_DESAP            Unreviewed;       813 AA.
AC   B1I307;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE            EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN   OrderedLocusNames=Daud_0863 {ECO:0000313|EMBL:ACA59376.1};
OS   Desulforudis audaxviator (strain MP104C).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforudis.
OX   NCBI_TaxID=477974 {ECO:0000313|EMBL:ACA59376.1, ECO:0000313|Proteomes:UP000008544};
RN   [1] {ECO:0000313|Proteomes:UP000008544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C {ECO:0000313|Proteomes:UP000008544};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA   Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT   "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACA59376.1, ECO:0000313|Proteomes:UP000008544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C {ECO:0000313|EMBL:ACA59376.1,
RC   ECO:0000313|Proteomes:UP000008544};
RX   PubMed=18845759; DOI=10.1126/science.1155495;
RA   Chivian D., Brodie E.L., Alm E.J., Culley D.E., Dehal P.S., Desantis T.Z.,
RA   Gihring T.M., Lapidus A., Lin L.H., Lowry S.R., Moser D.P.,
RA   Richardson P.M., Southam G., Wanger G., Pratt L.M., Andersen G.L.,
RA   Hazen T.C., Brockman F.J., Arkin A.P., Onstott T.C.;
RT   "Environmental genomics reveals a single-species ecosystem deep within
RT   Earth.";
RL   Science 322:275-278(2008).
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; CP000860; ACA59376.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1I307; -.
DR   STRING; 477974.Daud_0863; -.
DR   KEGG; dau:Daud_0863; -.
DR   eggNOG; COG0836; Bacteria.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_014562_0_0_9; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000008544; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008928; F:mannose-1-phosphate guanylyltransferase (GDP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004475; F:mannose-1-phosphate guanylyltransferase (GTP) activity; IEA:InterPro.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02509; GDP-M1P_Guanylyltransferase; 1.
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   InterPro; IPR049577; GMPP_N.
DR   InterPro; IPR005835; NTP_transferase_dom.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 1.
DR   Pfam; PF00483; NTP_transferase; 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; SSF159283; Guanosine diphospho-D-mannose pyrophosphorylase/mannose-6-phosphate isomerase linker domain; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
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:ACA59376.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:ACA59376.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008544};
KW   Transferase {ECO:0000313|EMBL:ACA59376.1}.
FT   DOMAIN          12..292
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   DOMAIN          364..477
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          514..613
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          618..726
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          733..805
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   813 AA;  90308 MW;  E283D921F0CCFD6C CRC64;
     MTASERRWFP VAVIMAGGVG TRFWPLSTED RPKQFLQLFG ERSLLQQTRD RLAAFVAPEH
     TLVLTNERFT YLVRAQLPEI PEANIIGEPA RRDTAGAVTL AALLCRRRFG DPAMIVLPAD
     HVIQPVEEFQ RVLASALEAA RREKALYAFG IPPTHPATGY GYLERGEKVL DDGGVVHYRL
     LRFKEKPDAE TARAYVDSGR FFWNSGIFVW TADTILEAVR KHLPGHLGVL EPLAALDGSD
     DWTTGLRRLF PLLPAVSIDY GVMEKAENVR AVAATFSWSD VGGWTALEPF LEKDTSNNAC
     RGRVRSLKAG SNIVFCEDPE ETVSLIGVRD LIVVRAGKQT LVVPRQRAEE LKELAEPKKR
     TVCFKAYDIR GRVPDDLNED IAYAVGQAYT ALFRPARVVV GRDVRHSSPP LSRALIRGLT
     DSGVDVLDIG LCGTEQVYFA TFDLGVDGGI MVTASHNPVD YNGMKLVRKE ARPVSGDSGL
     REMEALLAGG DLAARLPKRA RPPGRVTRVE IMDRYVAHLL RYVDVSILKP YKVVCNAGNG
     GAGLVIDALE KHLPFRFSKY FFEPDGTFPN GVPNPLLPEN RRVTSEAVLR EGADIGIAWD
     GDFDRCFLFD EKGAFVEGYY IVGLLAGHQL ALHPGAKIIH DPRLTWNTIE IVRQAGGIPV
     LNKTGHAFIK ERMRAEDAVY GGEMSAHHYF RDFAYCDSGM IPWLLVLEIM SRTGKPLSEL
     VGERMRLFPI SGEINRSVAD PAAVLARVRA RYEPEALNVD ETDGISLEFE RWRFNLRLSN
     TEPVVRLNVE TRGDEALLRQ KTAEILAEMD GQG
//
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