ID A0A371J6M3_9FIRM Unreviewed; 565 AA.
AC A0A371J6M3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Phosphoglucomutase {ECO:0000256|ARBA:ARBA00039995};
DE EC=5.4.2.2 {ECO:0000256|ARBA:ARBA00012728};
DE AltName: Full=Alpha-phosphoglucomutase {ECO:0000256|ARBA:ARBA00041467};
DE AltName: Full=Glucose phosphomutase {ECO:0000256|ARBA:ARBA00041398};
GN ORFNames=CHL78_005695 {ECO:0000313|EMBL:RDY28440.1};
OS Romboutsia weinsteinii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=2020949 {ECO:0000313|EMBL:RDY28440.1, ECO:0000313|Proteomes:UP000215694};
RN [1] {ECO:0000313|EMBL:RDY28440.1, ECO:0000313|Proteomes:UP000215694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-19649 {ECO:0000313|EMBL:RDY28440.1,
RC ECO:0000313|Proteomes:UP000215694};
RX PubMed=28982987;
RA Maheux A.F., Boudreau D.K., Berube E., Boissinot M., Cantin P., Raymond F.,
RA Corbeil J., Omar R.F., Bergeron M.G.;
RT "Draft Genome Sequence of Romboutsia weinsteinii sp. nov. Strain CCRI-
RT 19649(T) Isolated from Surface Water.";
RL Genome Announc. 5:e00901-17(2017).
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 -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005164}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:RDY28440.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NOJY02000007; RDY28440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371J6M3; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000215694; 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 InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
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 PRINTS; PR00509; PGMPMM.
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:UP000215694}.
FT DOMAIN 43..184
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 209..312
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 325..451
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 490..545
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 565 AA; 63277 MW; D73DB7CF17DA9EC2 CRC64;
MDYMKTYEEW MNNPYFDENT REELAKLKDD KKEIEDRFYK DLEFGTAGLR GVIAAGTNRI
NNYTVRRATF GLANYIIKNT TDEEKNRGVV IAHDNRHMSR EFCMEAANTL AACGIKAYIF
DSLRTTPELS FAVRNLHAIA GIVITASHNP PEYNGYKVYW EDGAQVMPHI ANTITEEINS
IKDYSTIPTI TEENKNLVIM LGEDDDTSFI EAVKKQVIRR DLVENIGKDF KIVYTPLCGT
GNVPIRRALK EVGFENILVV AEEEMPDPNF AGLDYPNPEE QKALNRGILL AKEQGADLVI
ATDPDCDRVG VAVKTTTGEY ALLTGNQIGG LLTNYIIEGL KEKNELKDNS ALIKTIVTSE
FGADIAKANN IEVMSVLTGF KFIGEKIKGF EETNSNTYLF GYEESYGYLV GTHARDKDGV
VASVLISEMA AFYYSKGMSL YEGLMELYKN YGFFKEKTIS ITLKGIEGLN KIQEIIAYFR
ENELSQLNNT KVVDSKDYKQ GIDGLPKADV LKYFLEDGSW VAVRPSGTEP KLKFYVAVKG
ADEAEADSKL NGINKDIDAL LEKLM
//
