ID A0A1I7GLL5_9FIRM Unreviewed; 564 AA.
AC A0A1I7GLL5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=SAMN02910342_00706 {ECO:0000313|EMBL:SFU49382.1};
OS Butyrivibrio sp. INlla21.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520811 {ECO:0000313|EMBL:SFU49382.1, ECO:0000313|Proteomes:UP000198910};
RN [1] {ECO:0000313|EMBL:SFU49382.1, ECO:0000313|Proteomes:UP000198910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INlla21 {ECO:0000313|EMBL:SFU49382.1,
RC ECO:0000313|Proteomes:UP000198910};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FPCC01000004; SFU49382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7GLL5; -.
DR STRING; 1520811.SAMN02910342_00706; -.
DR Proteomes; UP000198910; Unassembled WGS sequence.
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; cd05799; PGM2; 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 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}.
FT DOMAIN 43..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..311
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 324..450
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 492..537
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 564 AA; 63140 MW; 6D5B43514862F9EF CRC64;
MDYITRYNEW LTNLKDDDPL KAELLGIKGD DKEIEDRFYQ DLSFGTAGLR GKVGAGTNRM
NFLTVGKASQ GVAAYIVSKG KEAMDKGIVI AHDPRHFSKE FSMFAAGIFA ANGIKVYTFP
DLRPTPELAF MIRRLGTTSG INITASHNPK EYNGYKAYWD DGCQVSSDVA DGMTEEINKV
DIWTGIKTSD FDEGVKSGMI TVLSADYDRE YLDKIEGMAI HEGDELDLSI PLVYTPLNGC
GSIPFRQMLT DRGFTNWKIV PEQENPDPDF TTVGYPNPED PKAFKLSEQY GREFGAELLM
ATDPDADRFA IEIRDDNGNY IPLNGNQTGY LLVNYVLEGH KSAGTLPEKG AMVKSIVTST
LSTIMASAYG VEMFETLTGF KNICGKIPYL HENGYTYLFG YEESVGYAVC EDIRDKDGIS
AGMLVAEAAA YYRKQGKTLW DVLQEIYAKY GFFAEDEPNI VLEGIPGAQR IQRMMKWFRE
NIPSEVAGAK TEKVIDYING YEDIPPQNAI RIFLDNGSWF AIRPSGTEPK IKFYFYSNRN
SRENALLTNK QIKEEIFGLI NSVE
//