ID A0A0R2BH24_9LACO Unreviewed; 669 AA.
AC A0A0R2BH24;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=FC84_GL000809 {ECO:0000313|EMBL:KRM78551.1};
OS Lapidilactobacillus dextrinicus DSM 20335.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lapidilactobacillus.
OX NCBI_TaxID=1423738 {ECO:0000313|EMBL:KRM78551.1, ECO:0000313|Proteomes:UP000051813};
RN [1] {ECO:0000313|EMBL:KRM78551.1, ECO:0000313|Proteomes:UP000051813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20335 {ECO:0000313|EMBL:KRM78551.1,
RC ECO:0000313|Proteomes:UP000051813};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
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:KRM78551.1}.
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DR EMBL; AYYK01000016; KRM78551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2BH24; -.
DR STRING; 1423738.FC84_GL000809; -.
DR PATRIC; fig|1423738.3.peg.818; -.
DR Proteomes; UP000051813; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000051813}.
FT DOMAIN 137..276
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 305..409
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 421..548
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 598..655
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 669 AA; 74102 MW; D0B8660C58D0F28A CRC64;
MPAIIANYGE KVVPANVKNF LNKEILTQYG WQESVVSLCQ RYGLTGVFLS WHNFTVIGQV
QILERLSFRL VNPLQKSLFI LSKSVIMKLV MKGGFFMSWQ DNYQLWQNAE LTSDLKNDLA
EMAKDEDKLI EAFTKPMEFG TAGMRGVMEP GINAMNIYTV RQATEGLARF MDQLPAEQKA
AGVAISFDSR YHSQEFALNA AGVLGAHGIK SYVFDGLRPT PELSFTVRHL HTYAGIMITA
SHNPKQYNGY KIYGPDGGQM PPEEVNQIVA YIEKVTDLFS VKTLTQSELR AHNLMQLVGE
DIDEAYLAKL ATVTIRPDLI KKVASELSVV YSPLHGTGKV LYDRVFRTAG LTNVVVVPEQ
AVLDPEFATT PFPNPEFPQT FELAEQLGAK NGADLLIATD PDADRLGAAV RQPNGEYQLL
TGNQIAALMV NYILAAKQAI GELPADGCIV KSIVSSEFAA KVAASYGVET RDVLTGFKYI
GEQIEQMETT GQGHFLFGFE ESYGYLVKSF VRDKDAMQAS VMLAEVAAFY REQGKTMYDG
LQELFTKFGY FQEKTVSFDF LGLSGHEKMA NVMKEFRANP VTEVAGVAVV ATEDYQNQTK
TLADGTVEKL ELPTANVLKY YLTDETWIAV RPSGTEPKIK LYFGVESDSA ATSTAKIEKY
QADLATRLK
//
