DPH2_NEUCR
ID DPH2_NEUCR Reviewed; 602 AA.
AC Q7S5C0;
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 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=dph-2; ORFNames=NCU06168;
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=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: Required for the first step of diphthamide biosynthesis, a
CC post-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 (By similarity). Facilitates
CC the reduction of the catalytic iron-sulfur cluster found in the dph-1
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 dph-1 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 dph-1, dph-2, dph-3 and a NADH-dependent reductase,
CC predominantly cbr-1. {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; CM002242; EAA30794.1; -; Genomic_DNA.
DR RefSeq; XP_960030.1; XM_954937.2.
DR AlphaFoldDB; Q7S5C0; -.
DR SMR; Q7S5C0; -.
DR STRING; 5141.EFNCRP00000005390; -.
DR EnsemblFungi; EAA30794; EAA30794; NCU06168.
DR GeneID; 3876177; -.
DR KEGG; ncr:NCU06168; -.
DR VEuPathDB; FungiDB:NCU06168; -.
DR HOGENOM; CLU_015210_1_1_1; -.
DR InParanoid; Q7S5C0; -.
DR OMA; PFNNMYD; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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; -; 2.
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..602
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 2"
FT /id="PRO_0000083391"
FT REGION 445..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT BINDING 178
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
FT BINDING 401
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P32461"
SQ SEQUENCE 602 AA; 65335 MW; C5ED6ED9CD97A594 CRC64;
MAGELNAAPV LSTPEDHLFE YAVVPTDDQT KAKSDDELRD IYEITRTAKE VGEGGWRRIG
LQFPDHMLCD APRVVQLLEA ELASLPQPTV PTSTADLQST ATACPEPSTT NNGQCGRNVQ
QNGTGCGCGK QAPAPVESQP KARRVYVLAD TSYSACCVDE IAAEHVNADV VVHYGRSCLS
PTSRLPVIYV FTKHILDRDA ALVKFEKEYP DKEAKVVLMA DVTYQVHVPS LLSELQSGGY
VNLLATEIVH NPMGRIPNRK VVDAQGKEVE ISHGSETSTG LDLRDYSIFH ISQPPTALLL
ALCSRVKNLY IFQTSSDSSS LYSAQRLLGR RYARLLSLTT AGIIGILVNT LSVSNYLSSI
DSIRKQIAAA GKKSYTMVVG KLNPAKLANF AEIDGWVVVG CWESSLIEDD AGFYKPVITP
FELELALASD DERVWTGEWW GGIEAVKPPI DEKPGEKKSE ENENNEAQDT AGAEQASGDG
ELDSEEESAP PEFDWRTGKL VSHSRPMRMA ASKPKSAKKE DSSDKPDAPP RSSALTLRSK
AQELASVNGV VSPGAEYLRT QRTWVGLGTD FDEEASMTIE EGRGGVARGY TVGGEGEKHL
MS
