UniProt: A0A2I1FAI4

Database: UniProt
Entry: A0A2I1FAI4_9GLOM

LinkDB:  A0A2I1FAI4_9GLOM 
Original site:  A0A2I1FAI4_9GLOM

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (4)   
   EMBL (4)   
Protein domain (11)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (20)   

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ID   A0A2I1FAI4_9GLOM        Unreviewed;       378 AA.
AC   A0A2I1FAI4;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|ARBA:ARBA00012309, ECO:0000256|RuleBase:RU362016};
DE            EC=1.1.1.284 {ECO:0000256|ARBA:ARBA00012309, ECO:0000256|RuleBase:RU362016};
GN   ORFNames=RhiirA1_427350 {ECO:0000313|EMBL:PKC58910.1}, RhiirA4_438122
GN   {ECO:0000313|EMBL:PKY51223.1}, RhiirA5_318306
GN   {ECO:0000313|EMBL:PKB99575.1}, RhiirC2_841198
GN   {ECO:0000313|EMBL:PKK59176.1};
OS   Rhizophagus irregularis.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX   NCBI_TaxID=588596 {ECO:0000313|EMBL:PKC58910.1, ECO:0000313|Proteomes:UP000232688};
RN   [1] {ECO:0000313|Proteomes:UP000232722, ECO:0000313|Proteomes:UP000233469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4 {ECO:0000313|EMBL:PKY51223.1,
RC   ECO:0000313|Proteomes:UP000234323}, A5 {ECO:0000313|EMBL:PKB99575.1,
RC   ECO:0000313|Proteomes:UP000232722}, and C2
RC   {ECO:0000313|EMBL:PKK59176.1, ECO:0000313|Proteomes:UP000233469};
RA   Ropars J., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PKB99575.1, ECO:0000313|Proteomes:UP000232722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A5 {ECO:0000313|EMBL:PKB99575.1,
RC   ECO:0000313|Proteomes:UP000232722};
RA   Chen E.C., Morin E., Beaudet D., Noel J., Ndikumana S., Charron P.,
RA   St-Onge C., Giorgi J., Grigoriev I.V., Roux C., Martin F.M., Corradi N.;
RT   "Extensive intraspecific genome diversity in a model arbuscular mycorrhizal
RT   fungus.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000232688, ECO:0000313|Proteomes:UP000233469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1 {ECO:0000313|EMBL:PKC58910.1,
RC   ECO:0000313|Proteomes:UP000232688}, and C2
RC   {ECO:0000313|EMBL:PKK59176.1, ECO:0000313|Proteomes:UP000233469};
RA   Chen E.C.H., Morin E., Baudet D., Noel J., Ndikumana S., Charron P.,
RA   St-Onge C., Giorgi J., Grigoriev I.V., Roux C., Martin F.M., Corradi N.;
RT   "Extensive intraspecific genome diversity in a model arbuscular mycorrhizal
RT   fungus.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:PKC58910.1, ECO:0000313|Proteomes:UP000232688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1 {ECO:0000313|EMBL:PKC58910.1,
RC   ECO:0000313|Proteomes:UP000232688};
RA   Corradi N., Sedzielewska K., Noel J., Charron P., Farinelli L., Marton T.,
RA   Kruger M., Pelin A., Brachmann A., Corradi N.;
RT   "Genome analyses suggest a sexual origin of heterokaryosis in a supposedly
RT   ancient asexual fungus.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC         formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58758; EC=1.1.1.284;
CC         Evidence={ECO:0000256|ARBA:ARBA00001030,
CC         ECO:0000256|RuleBase:RU362016};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-
CC         formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58758; EC=1.1.1.284;
CC         Evidence={ECO:0000256|ARBA:ARBA00001646};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU362016};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000256|ARBA:ARBA00010902,
CC       ECO:0000256|RuleBase:RU362016}.
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:PKC58910.1}.
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DR   EMBL; LLXJ01002140; PKB99575.1; -; Genomic_DNA.
DR   EMBL; LLXH01001439; PKC58910.1; -; Genomic_DNA.
DR   EMBL; LLXL01003183; PKK59176.1; -; Genomic_DNA.
DR   EMBL; LLXI01000980; PKY51223.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:FUN_003644; -.
DR   VEuPathDB; FungiDB:GLOIN_2v1654796; -.
DR   VEuPathDB; FungiDB:RhiirA1_427350; -.
DR   OMA; IKGRSEM; -.
DR   OrthoDB; 1077476at2759; -.
DR   Proteomes; UP000232688; Unassembled WGS sequence.
DR   Proteomes; UP000232722; Unassembled WGS sequence.
DR   Proteomes; UP000233469; Unassembled WGS sequence.
DR   Proteomes; UP000234323; Unassembled WGS sequence.
DR   GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR   GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR   CDD; cd08300; alcohol_DH_class_III; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR014183; ADH_3.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   NCBIfam; TIGR02818; adh_III_F_hyde; 1.
DR   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU362016};
KW   NAD {ECO:0000256|RuleBase:RU362016};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362016};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234323};
KW   Zinc {ECO:0000256|RuleBase:RU362016}.
FT   DOMAIN          19..375
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   378 AA;  40544 MW;  3513B03C81C5BDA5 CRC64;
     MSTAGQVIKC KAAVAWGPGQ PLIIEEIEVA PPKKGEVRVK ILATGVCHTD AYTLSGKDPE
     GEWWPIVFGH EGGGIVESVG EGVTSVQPGD HVIPLYIPEC GQCKFCKSGK TNLCSIVRST
     QGRGLMPDET TRFTCKGQKL YHYMGCSTFS QYTVLSEISV AKINPKAPLD KVCLLGCGIT
     TGYGAATKTA NVQPGSTVAV FGCGGVGLSV IQGAAARKAS QIIAVDKNPK KFEYAKKLGA
     TDFVNPDDYD KPIQQVLIEM TDGGLDYTFE CIGNTKLMRA ALESCHKGWG ESIIIGVAGA
     GEEISTRPFQ LVTGRVWKGS AFGGVKGRSE LPSLVENYLE KKFEIDMFAT HQFKLGDINK
     AFEIMHDGDC IRAVISFE
//

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