ID   Q0F3C6_9PROT            Unreviewed;       544 AA.
AC   Q0F3C6;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:EAU56015.1};
GN   ORFNames=SPV1_04323 {ECO:0000313|EMBL:EAU56015.1};
OS   Mariprofundus ferrooxydans PV-1.
OC   Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC   Mariprofundaceae; Mariprofundus.
OX   NCBI_TaxID=314345 {ECO:0000313|EMBL:EAU56015.1, ECO:0000313|Proteomes:UP000005297};
RN   [1] {ECO:0000313|EMBL:EAU56015.1, ECO:0000313|Proteomes:UP000005297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PV-1 {ECO:0000313|EMBL:EAU56015.1,
RC   ECO:0000313|Proteomes:UP000005297};
RA   Emerson D., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (SEP-2006) 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, ECO:0000256|RuleBase:RU004326}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAU56015.1}.
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DR   EMBL; AATS01000001; EAU56015.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0F3C6; -.
DR   STRING; 314344.AL013_13185; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_045514_1_0_0; -.
DR   InParanoid; Q0F3C6; -.
DR   Proteomes; UP000005297; Unassembled WGS sequence.
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   CDD; cd03088; ManB; 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   PANTHER; PTHR42946:SF1; PHOSPHOGLUCOMUTASE (ALPHA-D-GLUCOSE-1,6-BISPHOSPHATE-DEPENDENT); 1.
DR   PANTHER; PTHR42946; PHOSPHOHEXOSE MUTASE; 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   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:UP000005297}.
FT   DOMAIN          48..172
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          222..319
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          324..443
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          473..532
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   544 AA;  58396 MW;  E43924E6553052B3 CRC64;
     MIIPAQDISL IAQNWQYRSC IRYRSGGHVM AVQSEQILIS SLMEESGVKF GTSGARGLAT
     DMTDRVCYAY TTAFLHYLES KGDIRRGDEV AIAGDYRPSS PRIMNAVALA VRDGGFLPVN
     CGFIPTPAVA CYAMARGQAS IMVTGSHIPD DRNGIKFYKP TGEVLKPDEE AISRSEVKLP
     ARFGVAGEVL ASCFDDDGEI LPDSMEGGCE ALPHVNTAAE TEYIQRYLDF FPAGCLQGRK
     VGVYQHSSVD RDIMVAVFEG LGASVTALGR SLSFIPVDTE AIRPEDVQLA SVWAEKGDFD
     CLVSADGDGD RPLISDEHGN WLRGDVAGIL CARYLEATHV VTPVSSNSAV EKSNWFKQVA
     RTRIGSPYVI EAMDMAVADG ASSVVGYEAN GGFLIATDIE LHGKTLTALP TRDAVIVPVA
     ILLLAIEGGV SVGGLLDSLP QRFSCSDRLK AFPTDIAQAR IKALSSGDIA TDKAAIEALF
     GEQFGTVASI NDTDGLRITF ASEEVVHLRP SGNAPELRCY NEAATEARAA EMNRICMAIM
     DGWR
//