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Database: UniProt
Entry: A0A062XAM2_9LACO
LinkDB: A0A062XAM2_9LACO
Original site: A0A062XAM2_9LACO 
ID   A0A062XAM2_9LACO        Unreviewed;       575 AA.
AC   A0A062XAM2;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=Lani381_0434 {ECO:0000313|EMBL:KDA46414.1};
OS   Ligilactobacillus animalis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1605 {ECO:0000313|EMBL:KDA46414.1, ECO:0000313|Proteomes:UP000027129};
RN   [1] {ECO:0000313|EMBL:KDA46414.1, ECO:0000313|Proteomes:UP000027129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=381-IL-28 {ECO:0000313|EMBL:KDA46414.1,
RC   ECO:0000313|Proteomes:UP000027129};
RA   Sturino J.M., Rajendran M., Altermann E.;
RT   "Draft Genome Sequence of Lactobacillus animalis 381-IL-28.";
RL   Submitted (APR-2014) 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   -!- 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, 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:KDA46414.1}.
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DR   EMBL; JMHU01000004; KDA46414.1; -; Genomic_DNA.
DR   RefSeq; WP_035447336.1; NZ_POVP01000003.1.
DR   AlphaFoldDB; A0A062XAM2; -.
DR   GeneID; 61226776; -.
DR   PATRIC; fig|1605.9.peg.434; -.
DR   eggNOG; COG1109; Bacteria.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000027129; 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, 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          326..453
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          511..558
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   575 AA;  63911 MW;  BA436365D50DB88C CRC64;
     MSWEETYTIW NKQPDLAPEV REDLDKIVND KEALEDAFYT PMEFGTAGMR GLIGAGINRM
     NIYTVRQATE GLARFMDTLD EETKLRGVAI SYDSRHMSQE FAFEAARVLG AHGIPSFVFE
     SLRPTPELSF TVRHLHAYAG IMITASHNPK QYNGYKIYGE DGAQMPPKES DMITNYIREV
     DDLFAVEVAD KDALINDGTL KVIGSEVDEV YLENAKEVTI DRELVAEEGK TMKLVFTPLH
     GTGGMLGEKA LRQAGFEDFT MVPEQAMPDP EFSTVEHPNP EFTEAFDLAI KLGKSQKADL
     LVAVDPDADR LGAAVRQPDG EYELLTGNQI AALMLNYILT ARKKAGNLPA NGALVKSIVS
     SEFAAKVAAD FGVEAINVLT GFKFIAEQIQ HFEETNEHSF MLGFEESYGY LIRPFVRDKD
     AIQSLVLLAE VAAFYKKQGK NLYDGLQELF EKYGYFAEKT IALTFDGIEG AQEIKDLMAK
     FRQELPTDFA GYKVIAAEDY QASSRQDAAG NVTAINLPKS NVLKYFLEDG TWIAVRPSGT
     EPKIKFYIGT QGDSEADAQA KCEKFEKAIN DFIKG
//
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