ID E8N4Y6_ANATU Unreviewed; 473 AA.
AC E8N4Y6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Phosphotransferase {ECO:0000313|EMBL:BAJ63500.1};
DE EC=5.4.2.- {ECO:0000313|EMBL:BAJ63500.1};
GN OrderedLocusNames=ANT_14720 {ECO:0000313|EMBL:BAJ63500.1};
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:BAJ63500.1, ECO:0000313|Proteomes:UP000008922};
RN [1] {ECO:0000313|EMBL:BAJ63500.1, 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, ECO:0000256|RuleBase:RU004326}.
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; AP012029; BAJ63500.1; -; Genomic_DNA.
DR RefSeq; WP_013559882.1; NC_014960.1.
DR AlphaFoldDB; E8N4Y6; -.
DR STRING; 926569.ANT_14720; -.
DR GeneID; 78349880; -.
DR KEGG; atm:ANT_14720; -.
DR eggNOG; COG1109; Bacteria.
DR HOGENOM; CLU_016950_7_1_0; -.
DR InParanoid; E8N4Y6; -.
DR OrthoDB; 9806956at2; -.
DR Proteomes; UP000008922; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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; 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; 2.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:BAJ63500.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008922};
KW Transferase {ECO:0000313|EMBL:BAJ63500.1}.
FT DOMAIN 6..139
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02878"
FT DOMAIN 164..265
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02879"
FT DOMAIN 272..377
FT /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF02880"
FT DOMAIN 414..459
FT /note="Alpha-D-phosphohexomutase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00408"
SQ SEQUENCE 473 AA; 51765 MW; D6465D5E81231D8E CRC64;
MSHTIRFGTD GWRGVIAEDY TFANVRCATQ GYASYMIRHG KAGATFVIGH DKRFHSENFA
LAAAEVMAGN GLKVLLTDGA TPTPVIAFSV VHHKAAGAIN ITASHNPPTD NGFKVRNEFG
GAIDPEGLKE IESLIPEDES EVKRMPASEA EAKGLIQRFD PAPAYIEHLK ELIDVEPIKQ
AGLKIVVDCM WGNGAGWFPR ILSGGKTEII EIHNERNPIF PEMKRPEPIP PNINVGLKKT
VDSGADVLLI TDGDADRVGV GDEKGNFINQ LQVYALLALY LLEVRGERGA IVKTLSTTSM
LEKLGKMYNI PVYETGVGFK YVAPKMLETN AMIGGEESGG YAFRGNVPER DGILAGLYIL
DMMVKLQRKP SELIDLLFSK VGPHFYDRID RTFTGERSAR EQAILAANPT TIGGLKVTGL
NTTDGFKFSL EDGGWLLIRF SGTEPIMRVY CETTHKDRVP YILKDGLKIA GLE
//
