ID A0A0F3RWE8_9LACO Unreviewed; 577 AA.
AC A0A0F3RWE8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=VC81_00105 {ECO:0000313|EMBL:KJW13919.1};
OS Levilactobacillus spicheri.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=216463 {ECO:0000313|EMBL:KJW13919.1, ECO:0000313|Proteomes:UP000033491};
RN [1] {ECO:0000313|EMBL:KJW13919.1, ECO:0000313|Proteomes:UP000033491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP38 {ECO:0000313|EMBL:KJW13919.1,
RC ECO:0000313|Proteomes:UP000033491};
RA Zheng J., Ganezle M.;
RL Submitted (MAR-2015) 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}.
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:KJW13919.1}.
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; JZCR01000002; KJW13919.1; -; Genomic_DNA.
DR RefSeq; WP_045806117.1; NZ_JZCR01000002.1.
DR AlphaFoldDB; A0A0F3RWE8; -.
DR STRING; 216463.VC81_00105; -.
DR PATRIC; fig|216463.3.peg.996; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000033491; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004614; F:phosphoglucomutase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KJW13919.1};
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 42..180
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 211..314
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 514..558
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 577 AA; 63517 MW; 719AF0F5FE2F635E CRC64;
MSWQENYAVW KNQATMLPDV RHELDAMAGN DDALEAAFSG PMSFGTAGMR GVMGPGIGQM
NVYTVRQATE GVARYLDTLD DATKQRGVAI SFDSRYHSTE FAHEAARVLG AHHIPSFVFD
DLRPTPELSF AVRHLHTAMG IMITASHNPK QYNGYKIYGP DGGQMPPKAS DKITEFVRSA
KDVFAIQVAD EQALRAAKVM HIIGENVDQA YLQNVVSVTI NHDLINQVGK TMKLIYTPLH
GTGKVIGERA LRKAGFENFT MVPEQAIADP EFPTVDFPNP EFPEAFDMAI ALGKQEGADL
LVATDPDADR LGAAVRQPDG EYQLLTGNQI ASILLAYILK ARKQAGQLPA NGRVVKSIVS
TELATKIAAA YGVEMKNVLT GFKFIAEQIH QYETTHDHTF LFGFEESYGY LIKPFVRDKD
AIQSTVLLAE VAADYKQRGM TLYDGIEELY ATYGYYAEKT TFEQFDGVDG AQQMAHLMSE
FRENAPQDFA GTTIDAVEDF STSTKTAADG TTSAIDLPQS NVLKYWLQDG TWICIRPSGT
EPKVKFYIGT SDHTAAAAQQ RLSTYEQALK DYVASVN
//
