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Database: UniProt
Entry: E8N302_ANATU
LinkDB: E8N302_ANATU
Original site: E8N302_ANATU 
ID   E8N302_ANATU            Unreviewed;       486 AA.
AC   E8N302;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Phosphotransferase {ECO:0000313|EMBL:BAJ65152.1};
DE            EC=5.4.2.- {ECO:0000313|EMBL:BAJ65152.1};
GN   OrderedLocusNames=ANT_31260 {ECO:0000313|EMBL:BAJ65152.1};
OS   Anaerolinea thermophila (strain DSM 14523 / JCM 11388 / NBRC 100420 /
OS   UNI-1).
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Anaerolinea.
OX   NCBI_TaxID=926569 {ECO:0000313|EMBL:BAJ65152.1, ECO:0000313|Proteomes:UP000008922};
RN   [1] {ECO:0000313|EMBL:BAJ65152.1, ECO:0000313|Proteomes:UP000008922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14523 / JCM 11388 / NBRC 100420 / UNI-1
RC   {ECO:0000313|Proteomes:UP000008922};
RA   Narita-Yamada S., Kishi E., Watanabe Y., Takasaki K., Ankai A., Oguchi A.,
RA   Fukui S., Takahashi M., Yashiro I., Hosoyama A., Sekiguchi Y., Hanada S.,
RA   Fujita N.;
RT   "Whole genome sequence of Anaerolinea thermophila UNI-1.";
RL   Submitted (DEC-2010) 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}.
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DR   EMBL; AP012029; BAJ65152.1; -; Genomic_DNA.
DR   RefSeq; WP_013561493.1; NC_014960.1.
DR   AlphaFoldDB; E8N302; -.
DR   STRING; 926569.ANT_31260; -.
DR   GeneID; 78351363; -.
DR   KEGG; atm:ANT_31260; -.
DR   eggNOG; COG1109; Bacteria.
DR   HOGENOM; CLU_016950_7_1_0; -.
DR   InParanoid; E8N302; -.
DR   OrthoDB; 9806956at2; -.
DR   Proteomes; UP000008922; Chromosome.
DR   GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd05800; PGM_like2; 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; 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; 2.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:BAJ65152.1};
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:UP000008922};
KW   Transferase {ECO:0000313|EMBL:BAJ65152.1}.
FT   DOMAIN          4..147
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          175..275
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02879"
FT   DOMAIN          279..389
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02880"
FT   DOMAIN          437..473
FT                   /note="Alpha-D-phosphohexomutase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00408"
SQ   SEQUENCE   486 AA;  53316 MW;  2B39280603DB66ED CRC64;
     MPIHFGTDGW RAVISDTFTF TNLRMVAQAI ADSIASGSWT DSLPTDRPID PKRMVVGFDT
     RFLSDRFAQE VARVLAANDF TVYLAQADAP TPAISYAVYH RNAIGGVMIT ASHNAPRYNG
     VKLKSYYGGS ALPDQCREVE VFLNDNEAKA RGPNLMEYEH ALEEKRIIRF NPIPEYYDHL
     RRLIDFDVIA SNPPRFVVDS MYGSGRGVIR GILQGTGCEV TEIRGEMNPG FGGVHPEPIA
     RYLGALAGAI GSGVGGFGIA TDGDADRTGA MDEHGNFVDP HKIMALSLRY LVEKRGMRGA
     VVRTVSTTRM IDRLCQKYNL PLYETPVGFN HIADYMMKDE VLIGGEESGG ISFKGHIPEG
     DGILMGLLIV EMVAAYRTTL RDLVEQLLAE VGPAHYERTD LRLRRPVSKS QMTARLVNEA
     PAEIGGERIV DVSTLDGVKY ILADDSWLLI RPSGTEPVLR VYAEGRSPQM VKALLGYGEQ
     VAASVV
//
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