ID A0A139SST5_9BACT Unreviewed; 677 AA.
AC A0A139SST5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Phosphoglucomutase {ECO:0000313|EMBL:KXU37594.1};
GN ORFNames=AXK11_02015 {ECO:0000313|EMBL:KXU37594.1};
OS Cephaloticoccus primus.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Cephaloticoccus.
OX NCBI_TaxID=1548207 {ECO:0000313|EMBL:KXU37594.1, ECO:0000313|Proteomes:UP000070058};
RN [1] {ECO:0000313|Proteomes:UP000070058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAG34 {ECO:0000313|Proteomes:UP000070058};
RA Sanders J.G., Lin J.Y., Wertz J.T., Russell J.A., Moreau C.S., Powell S.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KXU37594.1}.
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DR EMBL; LSZQ01000013; KXU37594.1; -; Genomic_DNA.
DR RefSeq; WP_068628739.1; NZ_LSZQ01000013.1.
DR AlphaFoldDB; A0A139SST5; -.
DR STRING; 1548207.AXK11_02015; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000070058; 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 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; 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; 2.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 4.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
FT DOMAIN 132..236
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 266..366
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 378..448
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 485..543
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
SQ SEQUENCE 677 AA; 72806 MW; E18A0BCF2AD09256 CRC64;
MTLLEKLETA AAEQKLLPTA LENLKKFLAA GLPAWAQESI GELVDAGQWA ELNDRFYAFI
SFGTGGMRGR TIGKVSTAAE RGETGADHAA IGSNLLNDFT LLRAVIGLYR YTQRYLAEGA
SAPAAAPAST LHATAAGASH APPRPRLVVA HDVRHFSRHF CELAASTWVK LGGEALIFDG
PRSTPQLSYT LRAQRAHAGI VITASHNPPH DNGFKAYFDD GAQIVPPHDS AVVAEVGAVP
LAELAVYLVK DLSEVVTLGA EADAGYRRAA RSALIDPEVL RRTKLRVVFT NIHGTGAIAS
VPLLEDAGCE VLTVPEQLAF DARFPSVKSP NPENAEALSL GVALAEARGA DVVMATDPDC
DRMGVAVRNR SGQMELLTGN QIGALLADYR LSQYKAQGLI PAAGSERACL LKTFVTTGLQ
DAIGAAHGVK VVNTLTGFKW ISAKLRRYEE QAARALAEAT SSAGSPNSGE AAPRLDSLGW
PERVRALQTH SAFLVLGSEE SYGYMPNDLV RDKDGNTACL MFAELCAALK ARGLTAGEAL
DELYLRHGFY LEGTINLYYE GASGKAKIDR ILASYRASPP KNFGEWRVTE FEDFGRQDFY
DADGERIPKQ DLYFVTLSNG YRFAARGSGT EPKMKFYLFA SEPVASAAEL PRVKAETRAT
LAELSEKIEA DARSRTE
//