ID B1IMJ8_CLOBK Unreviewed; 575 AA.
AC B1IMJ8;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
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 OrderedLocusNames=CLD_1425 {ECO:0000313|EMBL:ACA45006.1};
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA45006.1, ECO:0000313|Proteomes:UP000008541};
RN [1] {ECO:0000313|EMBL:ACA45006.1, ECO:0000313|Proteomes:UP000008541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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}.
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DR EMBL; CP000939; ACA45006.1; -; Genomic_DNA.
DR RefSeq; WP_003403335.1; NC_010516.1.
DR AlphaFoldDB; B1IMJ8; -.
DR KEGG; cbb:CLD_1425; -.
DR HOGENOM; CLU_016950_0_0_9; -.
DR Proteomes; UP000008541; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 42..179
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 222..312
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 324..451
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 518..558
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 575 AA; 66324 MW; 1E214760F60B0E36 CRC64;
MNYKYAYNSW MNSCFLEKRE KEQLKNIDDE QEIKDRFYKD LSFGTGGIRG VAGLGTNRIN
KYTIAKATEG LSNYLIHNFK EKGISVAIAY DCRNDSLDFA KKASEVLCSY GIRVYIFSDI
MCTPILSYAV RELKCKAGIV ITASHNSKEY NGYKVYNHNG NQITDKEAQE IAEYIKEVED
LGCIKYMDIN DAKEKNLYEF VPIEILNKYF YNVKNLTLRK DIVKNYEKNF KILYTPLHGT
GNVPVRRALC EIGYNNVFVV KDQEKPNGNF PTVKYPNPED NKAFYASLKE AENINPDVII
ATDPDCDRVG IMVRDHSTRY VALNGNELGV ILTNYILSSL EEEKKIPENS VLLKTIVTTD
MVKSICKDYG VKVEEVLTGF KYIGEKIEEF KKNGQNKFIF GFEESYGYLF GDFVREKDGI
ISSVLICEMA LYYKIQNKNL FDVLTELYDK YGYYKEKLIS MEFKGEEGKN KIENIINNLR
IHDSKTIFNE EILIKEDYKT GLKINMNKKK EYINKLPKSN VLKFHLNNGT NFVIRPSGTE
PKIKIYLSSV HTTAEGAEMK INKLEKNIKN MINKF
//
