ID A0A154BST2_ANASB Unreviewed; 550 AA.
AC A0A154BST2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) {ECO:0000256|ARBA:ARBA00012728};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
GN ORFNames=AXX12_02095 {ECO:0000313|EMBL:KYZ76957.1};
OS Anaerosporomusa subterranea.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Anaerosporomusa.
OX NCBI_TaxID=1794912 {ECO:0000313|EMBL:KYZ76957.1, ECO:0000313|Proteomes:UP000076268};
RN [1] {ECO:0000313|EMBL:KYZ76957.1, ECO:0000313|Proteomes:UP000076268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU4 {ECO:0000313|EMBL:KYZ76957.1,
RC ECO:0000313|Proteomes:UP000076268};
RA Choi J.K., Shah M., Yee N.;
RT "Anaerosporomusa subterraneum gen. nov., sp. nov., a spore-forming obligate
RT anaerobe isolated from saprolite.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000256|ARBA:ARBA00000443};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYZ76957.1}.
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DR EMBL; LSGP01000013; KYZ76957.1; -; Genomic_DNA.
DR RefSeq; WP_066238407.1; NZ_LSGP01000013.1.
DR AlphaFoldDB; A0A154BST2; -.
DR STRING; 1794912.AXX12_02095; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000076268; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05801; PGM_like3; 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; IPR005852; PGM_a-D-Glc-sp.
DR NCBIfam; TIGR01132; pgm; 1.
DR PANTHER; PTHR45745:SF1; PHOSPHOGLUCOMUTASE 2A-RELATED; 1.
DR PANTHER; PTHR45745; PHOSPHOMANNOMUTASE 45A; 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076268}.
FT DOMAIN 40..181
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 211..315
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 322..440
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 487..540
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 550 AA; 59651 MW; FCA64FDA98D6961A CRC64;
MSIHPLAGKK APKSLLVNIP RLISAYYANH PTADEPAQRV AFGTSGHRGN PLHNTFNEDH
IHAIVQAACC YRKTQAISGP LFLGFDTHAL SEPAFISALE VLAANGVETQ IAKEMNYTPT
PVISHAILSY NKGRTAGLAD GIVITPSHNP PDNGGIKYNP PNGGPADTTI TKWIADKANQ
LLQNNNQDVR RIQYEKALKT SQVREYDFIT PYVHDLRNII DMDAIRNAGL KLAADALGGS
GLAYWAPIAE TYRLDIDLIN GHPDPTFSFM NLDADGKIRM DCSSPYAMAG LIELKDKYDL
AFGNDPDFDR HGIVTRSVGL MNPNHYLATA IYYLFQNRPG WRNDAAIGKT LVSSSMIDRV
AVHLNKRLAE VPVGFKWFVD GLVDGSFGFG GEESAGASFL RKDGTVWTTD KDGFILCLLA
AEITAKTGRD PGHIYQSLTA NFGSPVYERI DSGANSRQKE VLAKLSPEQV TAETLAGEKI
TAKLTKAPSN NADIGGLKVC TANGWFAARP SGTEDVYKIY AESFTGAEHL RQIQAEAKQI
VASTFTAAGV
//
