ID DPH21_CANAL Reviewed; 529 AA. AC Q59SJ9; A0A1D8PL50; Q59JU1; Q59UP2; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2017, sequence version 2. DT 08-NOV-2023, entry version 89. DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2-1 {ECO:0000250|UniProtKB:P32461}; DE AltName: Full=Diphthamide biosynthesis protein 2-1 {ECO:0000305}; GN Name=DPH2; OrderedLocusNames=CAALFM_C400690CA; GN ORFNames=CaO19.11649, CaO19.1174, CaO19.4173; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP017626; AOW28861.1; -; Genomic_DNA. DR RefSeq; XP_712627.2; XM_707534.2. DR AlphaFoldDB; Q59SJ9; -. DR SMR; Q59SJ9; -. DR STRING; 237561.Q59SJ9; -. DR EnsemblFungi; C4_00690C_A-T; C4_00690C_A-T-p1; C4_00690C_A. DR GeneID; 3645752; -. DR KEGG; cal:CAALFM_C400690CA; -. DR CGD; CAL0000180772; orf19.11649. DR VEuPathDB; FungiDB:C4_00690C_A; -. DR HOGENOM; CLU_1111240_0_0_1; -. DR InParanoid; Q59SJ9; -. DR OrthoDB; 5491765at2759; -. DR UniPathway; UPA00559; -. DR Proteomes; UP000000559; Chromosome 4. 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:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017183; P:protein histidyl modification to diphthamide; ISS:UniProtKB. DR Gene3D; 3.40.50.11840; Diphthamide synthesis DPH1/DPH2 domain 1; 1. DR Gene3D; 3.40.50.11860; Diphthamide synthesis DPH1/DPH2 domain 3; 1. DR InterPro; IPR010014; DHP2. DR InterPro; IPR016435; DPH1/DPH2. DR InterPro; IPR042263; DPH1/DPH2_1. DR InterPro; IPR042265; DPH1/DPH2_3. DR NCBIfam; TIGR00322; diphth2_R; 1. DR NCBIfam; TIGR00272; DPH2; 1. DR PANTHER; PTHR10762:SF2; 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE SUBUNIT 2; 1. DR PANTHER; PTHR10762; DIPHTHAMIDE BIOSYNTHESIS PROTEIN; 1. DR Pfam; PF01866; Diphthamide_syn; 1. DR SFLD; SFLDG01121; Diphthamide_biosynthesis; 1. DR SFLD; SFLDF00408; Diphthamide_biosynthesis_famil; 1. DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1. PE 3: Inferred from homology; KW Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome. FT CHAIN 1..529 FT /note="2-(3-amino-3-carboxypropyl)histidine synthase FT subunit 2-1" FT /id="PRO_0000083384" FT BINDING 130 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P32461" FT BINDING 151 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P32461" FT BINDING 366 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000250|UniProtKB:P32461" SQ SEQUENCE 529 AA; 59198 MW; BA237CDDDE894163 CRC64; MTSETVIAPS LSTAQNDGTF TYDKVKSTAK ERKHLNLKNP SDANEIKSKI WNYYSLSELI QYLGQKENDD FKYKRITLQF PDNLICDSAT IVHELQRELN IVPQANQDTG ESNTAQRVWI LADTSYSACC VDEVAAEHVR SDLVVHFGDA CLNEIDKLQA VFVLGKPTLD VDAIVKQIKT AYSTEQKVVL MSDAPHTYLL PEIAKQLPDY DILIADLPKT SRAKIIGYTP PPTGHKKFNR VFNTDTVEFG KYELFHITSP ESPRLLQLTT NFASVTTYDP ISGTVSTGPF PNLMRRYKYV HQARMAGTVG ILVNTLSLAN TKVLLNTIKE KIKEAGKKHY IFVVGKPNVA KLANFESVDI WCILGCDHQG IIIDQINEYY KPIVTPYELL LGLSDELSWT GKWVVDYKSV LEEYGNEVIQ QNEDPDTDED LPPVFDPVTG RYVSTSKPLR QINHLMVTSS EQGGVDDHDN QLVKRFSNAV AIKGTVSTSA IHLQNRHWTG LGSDYTEDEN ATGALVEDGR KGIARGYDI //