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DPH2_CANGA
ID   DPH2_CANGA              Reviewed;         551 AA.
AC   Q6FPD9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000305};
DE   AltName: Full=Diphthamide biosynthesis protein 2;
DE   AltName: Full=Diphtheria toxin resistance protein 2 {ECO:0000305};
DE   AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 2 {ECO:0000305};
GN   Name=DPH2; OrderedLocusNames=CAGL0J04576g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Required for the first step of diphthamide biosynthesis, a
CC       post-translational modification of histidine which occurs in elongation
CC       factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group
CC       from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction
CC       is assisted by a reduction system comprising DPH3 and a NADH-dependent
CC       reductase, predominantly CBR1 (By similarity). Facilitates the
CC       reduction of the catalytic iron-sulfur cluster found in the DPH1
CC       subunit (By similarity). {ECO:0000250|UniProtKB:P32461}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P32461};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the
CC       reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
CC       {ECO:0000250|UniProtKB:P32461};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC       {ECO:0000250|UniProtKB:P32461}.
CC   -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase
CC       complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase,
CC       predominantly CBR1. {ECO:0000250|UniProtKB:P32461}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32461}.
CC   -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CR380956; CAG60854.1; -; Genomic_DNA.
DR   RefSeq; XP_447905.1; XM_447905.1.
DR   AlphaFoldDB; Q6FPD9; -.
DR   SMR; Q6FPD9; -.
DR   STRING; 5478.XP_447905.1; -.
DR   EnsemblFungi; CAG60854; CAG60854; CAGL0J04576g.
DR   GeneID; 2889446; -.
DR   KEGG; cgr:CAGL0J04576g; -.
DR   CGD; CAL0133634; CAGL0J04576g.
DR   VEuPathDB; FungiDB:CAGL0J04576g; -.
DR   eggNOG; KOG2648; Eukaryota.
DR   HOGENOM; CLU_015210_1_0_1; -.
DR   InParanoid; Q6FPD9; -.
DR   OMA; PFNNMYD; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR   Gene3D; 3.40.50.11840; -; 1.
DR   Gene3D; 3.40.50.11860; -; 1.
DR   InterPro; IPR010014; DHP2.
DR   InterPro; IPR016435; DPH1/DPH2.
DR   InterPro; IPR042263; DPH1/DPH2_1.
DR   InterPro; IPR042265; DPH1/DPH2_3.
DR   PANTHER; PTHR10762; PTHR10762; 1.
DR   PANTHER; PTHR10762:SF2; PTHR10762:SF2; 1.
DR   Pfam; PF01866; Diphthamide_syn; 1.
DR   SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR   TIGRFAMs; TIGR00322; diphth2_R; 1.
DR   TIGRFAMs; TIGR00272; DPH2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome.
FT   CHAIN           1..551
FT                   /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT                   subunit 2"
FT                   /id="PRO_0000083385"
FT   BINDING         116
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
FT   BINDING         137
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
FT   BINDING         371
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P32461"
SQ   SEQUENCE   551 AA;  61807 MW;  119AA0EAF51EF506 CRC64;
     MSNEDILVPA ALSTHQDESD FTFQKFDSDS MERSFYLGPL SSQDELWDKL MQYYSIDKLI
     AYLQRNPEYV QITLQFPDTL VKDSSFIIRA LQDKLDGDGA GRKFWALADT AYSACCVDEV
     AAEHVKGDLV IHFGDACLNA IQKLPVVYDF GKPFLDTDVL LACFTEEFKD KDQKICLMSN
     ASYTHHIPDL YSRLKSNGYT NVVYSVVNTG LLTETAEIID NTTPLSDTDE LFTLGNRVLM
     GARQEEDIDE ETLRNEYALF HITMPHDPHL LYLTTVFESI HTYDVADQVI SNGPYPSLTR
     RYKNMHKART AGCIGILVNT LSIRGTRETV NKLIKLIREN GKKHYLFVVG KPNVPKLANF
     EPVDIWCILG CGQSGIIVDE FGEFYKPIIT PYELTLALNF EVTWTGKWII DFQKAITEID
     NSLAELGIDD SKHGNDSDHD LDAPEFDAVT GKYVSSSRPL RALNHLQLDA PSNEDKQVMA
     RVNGGTVIKG TVSTAVEHLA NRAWTGLGSD YKDDEGYEED GATVEEGISG IARGYEFDQE
     DAARKSQNQS Q
 
 
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