ID A3LT21_PICST Unreviewed; 72 AA.
AC A3LT21;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Diphthamide biosynthesis protein 3 {ECO:0000256|ARBA:ARBA00041070};
GN ORFNames=PICST_45461 {ECO:0000313|EMBL:ABN65989.1};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65989.1, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN65989.1, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
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DR EMBL; CP000498; ABN65989.1; -; Genomic_DNA.
DR RefSeq; XP_001384018.1; XM_001383981.1.
DR AlphaFoldDB; A3LT21; -.
DR STRING; 322104.A3LT21; -.
DR GeneID; 4838950; -.
DR KEGG; pic:PICST_45461; -.
DR eggNOG; KOG2923; Eukaryota.
DR HOGENOM; CLU_155991_4_1_1; -.
DR InParanoid; A3LT21; -.
DR OMA; LFTYPCP; -.
DR OrthoDB; 1054714at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000002258; Chromosome 4.
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:UP000002258}.
FT DOMAIN 4..60
FT /note="DPH-type MB"
FT /evidence="ECO:0000259|PROSITE:PS51074"
SQ SEQUENCE 72 AA; 8411 MW; 22B907CC99C7F873 CRC64;
METIYDEIEI EDFTFDPITQ LFQYPCPCGD RFAISFDDLK DGEDIAVCPS CSLMVKVIYE
PEDLDEYEEE LK
//
