DPH21_CANAL
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 03-AUG-2022, entry version 84.
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}.
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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 PRIDE; Q59SJ9; -.
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; 750182at2759; -.
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: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..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
