ID I7LJJ8_METBM Unreviewed; 453 AA.
AC I7LJJ8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Phosphoglucomutase/phosphomannomutase {ECO:0000313|EMBL:CCJ36042.1};
DE EC=5.4.2.10 {ECO:0000313|EMBL:CCJ36042.1};
GN Name=manB {ECO:0000313|EMBL:CCJ36042.1};
GN OrderedLocusNames=BN140_1119 {ECO:0000313|EMBL:CCJ36042.1};
OS Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS (Methanogenium bourgense).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ36042.1, ECO:0000313|Proteomes:UP000009007};
RN [1] {ECO:0000313|Proteomes:UP000009007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC {ECO:0000313|Proteomes:UP000009007};
RX PubMed=22965103; DOI=10.1128/JB.01292-12;
RA Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT digester.";
RL J. Bacteriol. 194:5487-5488(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}.
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DR EMBL; HE964772; CCJ36042.1; -; Genomic_DNA.
DR RefSeq; WP_014867018.1; NC_018227.2.
DR AlphaFoldDB; I7LJJ8; -.
DR STRING; 1201294.BN140_1119; -.
DR GeneID; 13355142; -.
DR KEGG; mbg:BN140_1119; -.
DR PATRIC; fig|1201294.9.peg.1239; -.
DR HOGENOM; CLU_016950_7_1_2; -.
DR BioCyc; MBOU1201294:BN140_RS05585-MONOMER; -.
DR Proteomes; UP000009007; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd03087; PGM_like1; 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 InterPro; IPR024086; GlmM_arc-type.
DR NCBIfam; TIGR03990; Arch_GlmM; 1.
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 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:CCJ36042.1};
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:UP000009007}.
FT DOMAIN 6..135
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 154..253
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 261..370
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 389..450
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 453 AA; 48637 MW; 424F6D8C8AC58B01 CRC64;
MRNGKQMFGT NGVRGVVGEM MTPTLVLKIG AALGSMRNGT IAVGRDTRTS GEALAHALKA
GLLMTGCDVV DMGVLPTPAL QYIIKTDDRF AGGAMITASH NPPEYNGVKI IEADGTEMAD
DEIIRLEDRF FAGEFDAAAW DGVGTETAAP DRLEEYIQAV VGHFPAGIGK DMTVVVDPGS
GPAALTTPAI LERMGCRVHT INARLDGTFP GRMPEPTPEG LQPLSEMVIA TGADFGVAHD
GDADRAVFVD NKGRYIEENY EFGLIEDYVC SRNRGGLVVT PVATSRLIRD IAGKHGCTVD
YTPVGSIYVA RRMIELIGQG KNVSFGGEGN GGLIYSDHQF CRDGGMTAAM MVAVLASHNG
RDLSDIIDEL PVYHLVKEKY HAPDPAALVR AVEEALPEET IEKIDGIKII RDDAWALVRA
SGTEPMIRIM VESKDPGVAD TMYREIMQVV RQA
//
