ID G7VBM9_9CREN Unreviewed; 429 AA.
AC G7VBM9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=phosphomannomutase {ECO:0000256|ARBA:ARBA00012730};
DE EC=5.4.2.8 {ECO:0000256|ARBA:ARBA00012730};
GN ORFNames=P186_2254 {ECO:0000313|EMBL:AET33646.1};
OS Pyrobaculum ferrireducens.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET33646.1, ECO:0000313|Proteomes:UP000005867};
RN [1] {ECO:0000313|EMBL:AET33646.1, ECO:0000313|Proteomes:UP000005867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1860 {ECO:0000313|EMBL:AET33646.1,
RC ECO:0000313|Proteomes:UP000005867};
RX PubMed=22247528; DOI=10.1128/JB.06465-11;
RA Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT pyrobaculum able to grow with various electron acceptors.";
RL J. Bacteriol. 194:727-728(2012).
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; CP003098; AET33646.1; -; Genomic_DNA.
DR AlphaFoldDB; G7VBM9; -.
DR STRING; 1104324.P186_2254; -.
DR KEGG; pyr:P186_2254; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_9_1_2; -.
DR OrthoDB; 10363at2157; -.
DR BioCyc; PSP1104324:GJSN-2205-MONOMER; -.
DR Proteomes; UP000005867; 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 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:SF1; 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.
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}.
FT DOMAIN 3..125
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 148..238
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 243..348
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 360..420
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 429 AA; 47565 MW; A5121495032F69C1 CRC64;
MSVFKAYDIR GVVDSELTTE LVEKIGYAIS KFFNGEDVVV GMDVRTHSFR IAEALSRGLL
AGGSIVFIGT STTPITHFAS HLLQKPAVMI TASHNPPEYN GFKIMKSGGL DLESHEIQQL
ANLLEAPPAA RRGVVYTYDA LARYSEYIAR RFGKLNLAVG FDPANAAGVI LKPLLSQVFH
RLVAINDFPD GRFPAHLPDP EKAENLQQLR SLVVSNKLDV GIALDGDCDR VGIVTGRGEI
FRPEKMVYAL LNYYAKPGDV VVLDVTMPLY LEKVAEERGV KIVRQRVGHS FQKPTAVRHN
ALFWAEYSGH VGFRDHNYFD DGIYAALKLL STLGEAGVSL DKVLDTAPKI YEERLDIKAA
DPRKVVGDVK RRVANMEYYE IDGLDIRTKE GRLLIRPSNT EPVVRVKVES QTKEGLEKLK
SLLSQLTSP
//
