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DPH1_NEUCR
ID   DPH1_NEUCR              Reviewed;         459 AA.
AC   Q7SC98; V5IPM2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000305};
DE            EC=2.5.1.108 {ECO:0000250|UniProtKB:P40487};
DE   AltName: Full=Diphthamide biosynthesis protein 1;
DE   AltName: Full=Diphtheria toxin resistance protein 1 {ECO:0000305};
DE   AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1 {ECO:0000305};
GN   Name=dph-1; ORFNames=B18P7.020, NCU08503;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Catalyzes the first step of diphthamide biosynthesis, a post-
CC       translational modification of histidine which occurs in elongation
CC       factor 2. Dph-1 and dph-2 transfer a 3-amino-3-carboxypropyl (ACP)
CC       group from S-adenosyl-L-methionine (SAM) to a histidine residue, the
CC       reaction is assisted by a reduction system comprising dph-3 and a NADH-
CC       dependent reductase, predominantly cbr-1.
CC       {ECO:0000250|UniProtKB:P40487}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[translation elongation factor 2] + S-adenosyl-L-
CC         methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation
CC         elongation factor 2] + H(+) + S-methyl-5'-thioadenosine;
CC         Xref=Rhea:RHEA:36783, Rhea:RHEA-COMP:9748, Rhea:RHEA-COMP:9749,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:29979,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:73995; EC=2.5.1.108;
CC         Evidence={ECO:0000250|UniProtKB:P40487};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P40487};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000250|UniProtKB:P40487};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC   -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase
CC       complex composed of dph-1, dph-2, dph-3 and a NADH-dependent reductase,
CC       predominantly cbr-1. {ECO:0000250|UniProtKB:P40487}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40487}.
CC   -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BX842594; CAE75675.1; -; Genomic_DNA.
DR   EMBL; CM002237; ESA43685.1; -; Genomic_DNA.
DR   EMBL; CM002237; ESA43686.1; -; Genomic_DNA.
DR   RefSeq; XP_011393622.1; XM_011395320.1.
DR   RefSeq; XP_011393623.1; XM_011395321.1.
DR   AlphaFoldDB; Q7SC98; -.
DR   SMR; Q7SC98; -.
DR   STRING; 5141.EFNCRP00000008474; -.
DR   EnsemblFungi; ESA43685; ESA43685; NCU08503.
DR   EnsemblFungi; ESA43686; ESA43686; NCU08503.
DR   GeneID; 3879572; -.
DR   KEGG; ncr:NCU08503; -.
DR   VEuPathDB; FungiDB:NCU08503; -.
DR   HOGENOM; CLU_037146_1_1_1; -.
DR   InParanoid; Q7SC98; -.
DR   OMA; PGQVLGC; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
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; 3.40.50.11850; -; 1.
DR   Gene3D; 3.40.50.11860; -; 1.
DR   InterPro; IPR016435; DPH1/DPH2.
DR   InterPro; IPR042263; DPH1/DPH2_1.
DR   InterPro; IPR042264; DPH1/DPH2_2.
DR   InterPro; IPR042265; DPH1/DPH2_3.
DR   PANTHER; PTHR10762; PTHR10762; 1.
DR   Pfam; PF01866; Diphthamide_syn; 1.
DR   SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR   TIGRFAMs; TIGR00322; diphth2_R; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..459
FT                   /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT                   subunit 1"
FT                   /id="PRO_0000083377"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         165
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O58832"
FT   BINDING         268
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O58832"
FT   BINDING         403
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O58832"
SQ   SEQUENCE   459 AA;  50430 MW;  14A71074E4553B87 CRC64;
     MEDDRAQVDL GIAADIDEMN PPPPPSVQQK QPKKRFLGRQ SAAAGKSSSS SSNSTSQPAG
     ANTSIEDSGA IQVAQPRRAP RMLNQVPDSI LHDAALNEAI ALLPSNYSFE IHKTIHRIRT
     LDAKRVALQM PEGLLLFATT ISDILTQFCP GIETLIMGDV TYGACCIDDY TARAMGCDLL
     VHYAHSCLIP VDVTKIKTLY VFVDISIDTS HLLATLERNF APGKSIAMVG TIQFNATIHG
     VRSTLQKAGY EVIIPQIAPL SKGEILGCTS PNLSQFLTSS GKQVDMILYL GDGRFHLESI
     MIHNPSIPAY RYDPYSRKLT HETYGHEEMQ DVRRSAIRQA KTAKKWGLIL GSLGRQGNPN
     TLGLIEEKLK ANGTPFVNFC LSEIFPGKLA MMSDVECWVQ VACPRLSIDW GYAFPRPLLT
     PYEALIALEE KEDWGKGAYP MDYYGREGLG RTKPAAMEV
 
 
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