ID A0A437STQ0_9LACO Unreviewed; 574 AA.
AC A0A437STQ0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=EJK17_08505 {ECO:0000313|EMBL:RVU70275.1};
OS Lactobacillus xujianguonis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=2495899 {ECO:0000313|EMBL:RVU70275.1, ECO:0000313|Proteomes:UP000288291};
RN [1] {ECO:0000313|EMBL:RVU70275.1, ECO:0000313|Proteomes:UP000288291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT111-2 {ECO:0000313|EMBL:RVU70275.1,
RC ECO:0000313|Proteomes:UP000288291};
RA Meng J.;
RL Submitted (DEC-2018) 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}.
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:RVU70275.1}.
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DR EMBL; RXIA01000024; RVU70275.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437STQ0; -.
DR Proteomes; UP000288291; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000288291}.
FT DOMAIN 43..179
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 210..319
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 327..453
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 510..553
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 574 AA; 64227 MW; 2F62D96C99D295D4 CRC64;
MDAQETFAEW KKANNLPDYL QEQLETLGQD PKWVDDAFGQ DINFGTAGMR GKLEPGTNRI
NLFTVSRVTE GLARLIDENG EAAKKRGVAI SFDSRYHSRE FAEQAARILA THGIHVYLFD
DLRPTPELSF AVRYLHTFAG INITASHNAK QYNGYKAYGE DGAQMAPENA DRLFSYAQKV
TDIFHIKADS VLKLRANGTL QLIGEDVDEA YLNELKAVNI DQDLIKQNAD KLKIIYTPLH
GTGKMLYDRA FRQGGFDNVI PVPSQSIVDP EFPTTIKPNP EYRDVFKPGF KLADEVNANV
IIATDPDADR MGAAVRKEDG TFQVLTGNQI ATLMAYYLLV HLKESGKLAN DYEIVTSVVS
SALPFKIAKD FGIKTKHVLT GFKYIGEEVD RMKKVNDGKF LMGFEESYGY LFKPFARDKD
AMQGALMFAE VATYYASRGM TVFDGLQEIW QKYGVAYEIT RAIEMPGIGG QKKMAALMSK
LRDEHLTEIN GAKVLKIQDF LKKETITNGK TTPLEDFPES NVLKYFLDDE TWVALRPSGT
EPVIKAYVGV NKKDIQTAEQ AAKDYQAALA NLLK
//
