DPH1_NEMVE
ID DPH1_NEMVE Reviewed; 465 AA.
AC A7SLX5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000305};
DE EC=2.5.1.108 {ECO:0000250|UniProtKB:Q5NCQ5};
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=dph1; ORFNames=v1g246101;
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6;
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
CC -!- FUNCTION: Catalyzes the first step of diphthamide biosynthesis, a post-
CC translational modification of histidine which occurs in elongation
CC factor 2 (By similarity). Dph1 and dph2 transfer a 3-amino-3-
CC carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a
CC histidine residue, the reaction is assisted by a reduction system
CC comprising dph3 and a NADH-dependent reductase (By similarity).
CC {ECO:0000250|UniProtKB:P40487, ECO:0000250|UniProtKB:Q5NCQ5}.
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:Q5NCQ5};
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 dph1, dph2, dph3 and a NADH-dependent reductase.
CC {ECO:0000250|UniProtKB:P40487}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; DS469703; EDO35280.1; -; Genomic_DNA.
DR RefSeq; XP_001627380.1; XM_001627330.1.
DR AlphaFoldDB; A7SLX5; -.
DR SMR; A7SLX5; -.
DR STRING; 45351.EDO35280; -.
DR EnsemblMetazoa; EDO35280; EDO35280; NEMVEDRAFT_v1g246101.
DR eggNOG; KOG2648; Eukaryota.
DR HOGENOM; CLU_037146_1_1_1; -.
DR InParanoid; A7SLX5; -.
DR OMA; PGQVLGC; -.
DR OrthoDB; 750182at2759; -.
DR PhylomeDB; A7SLX5; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
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 Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..465
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 1"
FT /id="PRO_0000329957"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT BINDING 230
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT BINDING 357
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
SQ SEQUENCE 465 AA; 51299 MW; A6CB4A5364901528 CRC64;
MADSVEQSSV TTKRISAKGA RKRFVGTKSA SGKHSQGVDR VGSAAHRPVN QIPEEILKDT
KLQEALPENY NFEIHKTIWR IQQVKAKRVA LQFPEGLLLF ACTIADILES FTGCETVIMG
DVTYGACCVD DYSARALGCD LLVHYGHSCL VPIDATAGIK MLYVFVDIKI DTAHFVESVR
FNLGAGSCLA LVSTIQFVAA LQAASNELSK DYQVEIPQCK PLSPGEILGC TAPMLKDKDA
VIYLGDGRFH LEAVMIANPA IQAYRYDPYD KTFSKEYYDI DKMHEARQTA IKQASLASKY
GLILGTLGRQ GSPKVLQTLE KQLQSLNMDY IIVLLSEVFP DKLKLFKDVD AWVQVACPRL
SIDWGTAFPK PLLSPYEASV ALQSVAWQQS YPMDFYAYSS LGGWTPNNES NRPTPANRRK
KNLHTEVIID NVSDSKPVIK ESECGSGETC CGKCTKETDK HSSTP
