ID H8Z750_9GAMM Unreviewed; 493 AA.
AC H8Z750;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 08-OCT-2025, entry version 50.
DE SubName: Full=Phosphomannomutase {ECO:0000313|EMBL:EIC20849.1};
GN ORFNames=Thi970DRAFT_04515 {ECO:0000313|EMBL:EIC20849.1};
OS Thiorhodovibrio frisius.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Chromatiales; Chromatiaceae; Thiorhodovibrio.
OX NCBI_TaxID=631362 {ECO:0000313|EMBL:EIC20849.1, ECO:0000313|Proteomes:UP000002964};
RN [1] {ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Overmann J.,
RA Frigaard N.-U., Bryant D.A., Woyke T.J.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIC20849.1, ECO:0000313|Proteomes:UP000002964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=970 {ECO:0000313|EMBL:EIC20849.1,
RC ECO:0000313|Proteomes:UP000002964};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Zhang X., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Overmann J., Frigaard N.-U., Bryant D., Woyke T.;
RL Submitted (NOV-2011) 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}.
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DR EMBL; JH603170; EIC20849.1; -; Genomic_DNA.
DR RefSeq; WP_009151252.1; NZ_CP121471.1.
DR AlphaFoldDB; H8Z750; -.
DR STRING; 631362.Thi970DRAFT_04515; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_045514_1_0_6; -.
DR OrthoDB; 9803322at2; -.
DR Proteomes; UP000002964; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:TreeGrafter.
DR GO; GO:0004615; F:phosphomannomutase activity; IEA:TreeGrafter.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:TreeGrafter.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:TreeGrafter.
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; 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; IPR050060; Phosphoglucosamine_mutase.
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; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002964}.
FT DOMAIN 12..137
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 273..391
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 423..482
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 493 AA; 52633 MW; FBFFC1A991426170 CRC64;
MQIGDLMMTS GVKFGTSGAR GRVADMTDAV CYSYASGFLS YLSETGRLET GAPVALAGDY
RESTGRILAA CAQAVRDAGC EPRYFGRIPA PALATFSFAA GMPSMMVTGS HIPEDRNGIK
FNLPAGEILK DDEAGIAHQR VVLPPDLFDE AGSFRAGSPA LPAQTDAARE AYQRRFLDFF
PRDCLAGLRI GLYEHSTVAR DPLFEILSGL GADVTRLGFS ATFVPVDTEA IRAEDRDLAR
DWCAGGDFDA LVSADGDGDR PLLADASGRW LRGDVAGILC ARALGAAAIA TPVSCNTAVD
RLGEFSRVYR TRIGSPYVIA GMKTLIDDGH RPVVGYEANG GFLIASCIER QGRLLPALPT
RDAAIVAVAV LADAKARGLS LVELCAGLPP RFTDSDRIKD FPVDLSRERL GAFNTSDPSA
DCQAFAAAFG DVFAPVVAID HTDGVRATLS NGEILHLRPS GNAPELRAYT EADTPERANE
MNRQCMRVLQ DWR
//
