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Database: UniProt
Entry: A0A1I7GLL5_9FIRM
LinkDB: A0A1I7GLL5_9FIRM
Original site: A0A1I7GLL5_9FIRM 
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
//
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