ID A0A1Y1S511_9MICR Unreviewed; 83 AA.
AC A0A1Y1S511;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Diphthamide biosynthesis protein 3 {ECO:0000256|ARBA:ARBA00041070};
GN Name=DPH3 {ECO:0000313|EMBL:ORD93475.1};
GN ORFNames=ECANGB1_2174 {ECO:0000313|EMBL:ORD93475.1};
OS Enterospora canceri.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Enterocytozoonidae;
OC Enterospora.
OX NCBI_TaxID=1081671 {ECO:0000313|EMBL:ORD93475.1, ECO:0000313|Proteomes:UP000192639};
RN [1] {ECO:0000313|EMBL:ORD93475.1, ECO:0000313|Proteomes:UP000192639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB1 {ECO:0000313|EMBL:ORD93475.1,
RC ECO:0000313|Proteomes:UP000192639};
RX PubMed=28345194; DOI=10.1111/1462-2920.13734;
RA Wiredu Boakye D., Jaroenlak P., Prachumwat A., Williams T.A., Bateman K.S.,
RA Itsathitphaisarn O., Sritunyalucksana K., Paszkiewicz K.H., Moore K.A.,
RA Stentiford G.D., Williams B.A.;
RT "Decay of the glycolytic pathway and adaptation to intranuclear parasitism
RT within Enterocytozoonidae microsporidia.";
RL Environ. Microbiol. 19:2077-2089(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 [3Fe-4S](0)-[protein] + 2 Fe(2+)-[Dph3] + NADH = 2 [4Fe-
CC 4S](1+)-[protein] + 2 [Dph3] + H(+) + NAD(+); Xref=Rhea:RHEA:71239,
CC Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:17998, Rhea:RHEA-COMP:18001,
CC Rhea:RHEA-COMP:18002, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:33723, ChEBI:CHEBI:47402, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:83228;
CC Evidence={ECO:0000256|ARBA:ARBA00036715};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[3Fe-4S](1+)-[protein] + Fe(2+)-[Dph3] = [3Fe-4S](0)-[protein]
CC + Fe(3+)-[Dph3]; Xref=Rhea:RHEA:71235, Rhea:RHEA-COMP:17996,
CC Rhea:RHEA-COMP:17997, Rhea:RHEA-COMP:18002, Rhea:RHEA-COMP:18003,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33751,
CC ChEBI:CHEBI:47402, ChEBI:CHEBI:83228;
CC Evidence={ECO:0000256|ARBA:ARBA00036267};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156}.
CC -!- SIMILARITY: Belongs to the DPH3 family.
CC {ECO:0000256|ARBA:ARBA00024032}.
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:ORD93475.1}.
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DR EMBL; LWDP01000078; ORD93475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1S511; -.
DR VEuPathDB; MicrosporidiaDB:ECANGB1_2174; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000192639; Unassembled WGS sequence.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.10.660.10; DPH Zinc finger; 1.
DR InterPro; IPR007872; DPH_MB_dom.
DR InterPro; IPR036671; DPH_MB_sf.
DR PANTHER; PTHR21454:SF31; DPH3 HOMOLOG; 1.
DR PANTHER; PTHR21454; DPH3 HOMOLOG-RELATED; 1.
DR Pfam; PF05207; zf-CSL; 1.
DR SUPFAM; SSF144217; CSL zinc finger; 1.
DR PROSITE; PS51074; DPH_MB; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000192639}.
FT DOMAIN 20..76
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
SQ SEQUENCE 83 AA; 9771 MW; 9D33EE75B03B72D1 CRC64;
MEREFSYDQY FEQAADYVSH YDQIHLSEFE YDDECGTYTY PCPCGDDFVI TVDEIRNGET
IARCQSCSLI VLCLYDIDSK MMM
//
