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Database: UniProt
Entry: E1ZGQ9_CHLVA
LinkDB: E1ZGQ9_CHLVA
Original site: E1ZGQ9_CHLVA 
ID   E1ZGQ9_CHLVA            Unreviewed;       421 AA.
AC   E1ZGQ9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Alpha-D-phosphohexomutase alpha/beta/alpha domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CHLNCDRAFT_52755 {ECO:0000313|EMBL:EFN54798.1};
OS   Chlorella variabilis (Green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX   NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN   [1] {ECO:0000313|EMBL:EFN54798.1, ECO:0000313|Proteomes:UP000008141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NC64A {ECO:0000313|EMBL:EFN54798.1,
RC   ECO:0000313|Proteomes:UP000008141};
RX   PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA   Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA   Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA   Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT   "The Chlorella variabilis NC64A genome reveals adaptation to
RT   photosymbiosis, coevolution with viruses, and cryptic sex.";
RL   Plant Cell 22:2943-2955(2010).
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC       {ECO:0000256|ARBA:ARBA00010231}.
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DR   EMBL; GL433846; EFN54798.1; -; Genomic_DNA.
DR   RefSeq; XP_005846900.1; XM_005846838.1.
DR   AlphaFoldDB; E1ZGQ9; -.
DR   STRING; 554065.E1ZGQ9; -.
DR   GeneID; 17354496; -.
DR   KEGG; cvr:CHLNCDRAFT_52755; -.
DR   eggNOG; KOG2537; Eukaryota.
DR   InParanoid; E1ZGQ9; -.
DR   OrthoDB; 1475at2759; -.
DR   Proteomes; UP000008141; 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   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 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; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR049023; AMG1_II.
DR   PANTHER; PTHR45955; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR   PANTHER; PTHR45955:SF1; PHOSPHOACETYLGLUCOSAMINE MUTASE; 1.
DR   Pfam; PF21405; AMG1_II; 1.
DR   Pfam; PF02878; PGM_PMM_I; 2.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008141}.
FT   DOMAIN          48..91
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          102..173
FT                   /note="Alpha-D-phosphohexomutase alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF02878"
FT   DOMAIN          180..282
FT                   /note="Phosphoacetylglucosamine mutase AMG1"
FT                   /evidence="ECO:0000259|Pfam:PF21405"
SQ   SEQUENCE   421 AA;  44082 MW;  E8ADE887C2F98FDF CRC64;
     MAVPSVEQAV CSASRSYVLP AGFRPSYGTA GFRAVADLLH STMCGIMMAA RALKTQQITG
     ICITASHNPA PDNGVKLVEP SGEMLCQEWE SYANELANAQ TDAELAKQVA GLLAAEGITA
     PAPGVVMIAH DTRPSGPELA AAAAAGVRCL GAEPQMCGLL TTPQLHWMVM RRNLGQPCGE
     ADYHAALAGA YRQLVEGTAP LGQTLYMDCA NGVGAPKMAA LVASLAQADA GLAVDLRNTG
     QGVLNGGCGS DFLQKDRQLP ANFQDVPPGA RCCAVDGDSD RLMYFTPLEG GEKGEGDLET
     VSAAHAKTVI LLHPDKDEQL DASLVIPTCS ALEMQAAEVH KTATLLGLQS CRSHPSTTLR
     RQRVVLQNPD VPPLDRSSEA QQATRTIAGV VQRSLPPAAN MKLVEVNGRF EACCMGCRAK
     A
//
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