ID D3PC91_DEFDS Unreviewed; 474 AA.
AC D3PC91;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:BAI80214.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:BAI80214.1};
GN OrderedLocusNames=DEFDS_0735 {ECO:0000313|EMBL:BAI80214.1};
OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS SSM1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Deferribacteraceae; Deferribacter.
OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI80214.1, ECO:0000313|Proteomes:UP000001520};
RN [1] {ECO:0000313|EMBL:BAI80214.1, ECO:0000313|Proteomes:UP000001520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC {ECO:0000313|Proteomes:UP000001520};
RX PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA Takai K.;
RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT the genome sequence of the thermophilic bacterium Deferribacter
RT desulfuricans SSM1.";
RL DNA Res. 17:123-137(2010).
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; AP011529; BAI80214.1; -; Genomic_DNA.
DR AlphaFoldDB; D3PC91; -.
DR STRING; 639282.DEFDS_0735; -.
DR KEGG; ddf:DEFDS_0735; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_0; -.
DR Proteomes; UP000001520; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR005841; Alpha-D-phosphohexomutase_SF.
DR PANTHER; PTHR43771:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:BAI80214.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001520}.
FT DOMAIN 6..136
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 164..261
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 266..379
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 386..468
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 474 AA; 53979 MW; CF9CA894F1C66760 CRC64;
MIDRGIFRQY DIRGVVPDNF NKEVIKQIAN TFAYQVKEET GKENPTVTVG RDVRLSSDEL
FEGVKEGLID AGVNVVELGR CPTPVTYFSA FHLNPDGFIM ITGSHNPPEY NGMKFGIGKT
TFHSEKIQSV YENIMKYGYR KSDKKGTVSN YDIVSAYIDW NVEHFKELKE KIDNLGKKIK
VVIDAGNGVA SRVAPEIFKR LGVDTVELYC EEDGRFPNHH PDPTVEANLK DLIETVKKES
ADFGIGYDGD ADRIGVVDES GNIVWGDMLL IVYTKELKKF YEKPKVIADV KASQVFFDYA
KKIGAEPIMW KTGHSLIKNK LKETNAELAG EMSGHIFFND RYFGYDDAIY SSVRFLEAYV
NNLIDKKVEK VSDLLSDVPK VYNTPEIRFE CPEDKKFEIV KKLTELFKEY KDNGKYNIKD
IIDIDGIRVI FEDGWGLLRA SNTQPVLVMR FEASSKDKMA EYQNIIESEL KNLI
//
