ID D6CPG2_THIA3 Unreviewed; 458 AA.
AC D6CPG2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:CAZ87892.1};
DE EC=5.4.2.8 {ECO:0000313|EMBL:CAZ87892.1};
GN Name=manB {ECO:0000313|EMBL:CAZ87892.1};
GN OrderedLocusNames=THI_1199 {ECO:0000313|EMBL:CAZ87892.1};
OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ87892.1, ECO:0000313|Proteomes:UP000002372};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3As;
RA Genoscope - CEA;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22701 / CIP 110005 / 3As
RC {ECO:0000313|Proteomes:UP000002372};
RX PubMed=20195515; DOI=10.1371/journal.pgen.1000859;
RA Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M.,
RA Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V.,
RA Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J.,
RA Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C.,
RA Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P.,
RA Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E.,
RA Weiss S., Weissenbach J., Medigue C., Bertin P.N.;
RT "Structure, function, and evolution of the Thiomonas spp. genome.";
RL PLoS Genet. 6:E1000859-E1000859(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, ECO:0000256|RuleBase:RU004326}.
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DR EMBL; FP475956; CAZ87892.1; -; Genomic_DNA.
DR RefSeq; WP_013105238.1; NZ_CTRL01000016.1.
DR AlphaFoldDB; D6CPG2; -.
DR KEGG; thi:THI_1199; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_9_1_4; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000002372; 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: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.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CAZ87892.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002372}.
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 255..356
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 392..447
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 458 AA; 48876 MW; 167BD38EB059924F CRC64;
MAQLDPTIFK AYDIRGIVGK TLTEDACRAI GQAFATLARR NGETAVNISR DGRLSGPALA
QALSDGLRAG GVDVIDLGMN ATPMLYYACA TTPVVSGIQI TGSHNPPEYN GLKMVLGGNA
LFGEQIQELL ALTRSEAFAQ GQGSARQASI VEDYLGRIEG DIKLARPMKV VVDCGNGVSG
AFAPRLLRSL GCEVVELYCE VDGTFPNHHP DPADPRNLED LIRTVLDTGA ELGLAFDGDG
DRLGVVTPSG AVIWPDRQLM LYAADVLERH PGAPILFDVK CTAQLPAWVR RHGGEPVMGR
TGHSLVKAKM KEIDAPLAGE MSGHIFFKDR WYGFDDAQYG AARLLEILSR AENAGAVLEA
LPDSVSTPEL KLQTAEGANF TLCERLQREG RFPGASNIST IDGVRADYAD GFGLARPSNT
TPCVVLRFEG ADAAALARIQ AEFRAALLAL DASLILPF
//
