DPH1_PENVA
ID DPH1_PENVA Reviewed; 423 AA.
AC Q3T7C9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 43.
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};
DE AltName: Full=Tumor suppressor-like protein;
DE Short=TSL;
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA He F., Khadijah S., Manopo I., Xie Q., Kwang J.;
RT "White spot syndrome virus ORF222 is a ring-finger-dependant ubiquitin
RT protein ligase for a shrimp tumor-suppressor-like protein.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP UBIQUITINATION, AND INTERACTION WITH WHITE SPOT SYNDROME VIRUS E3
RP UBIQUITIN-PROTEIN LIGASE WSSV222.
RX PubMed=16571805; DOI=10.1128/jvi.80.8.3884-3892.2006;
RA He F., Fenner B.J., Godwin A.K., Kwang J.;
RT "White spot syndrome virus open reading frame 222 encodes a viral E3 ligase
RT and mediates degradation of a host tumor suppressor via ubiquitination.";
RL J. Virol. 80:3884-3892(2006).
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 (By
CC similarity). Interacts with white spot syndrome virus E3 ubiquitin-
CC protein ligase WSSV222. {ECO:0000250|UniProtKB:P40487,
CC ECO:0000269|PubMed:16571805}.
CC -!- PTM: Polyubiquitinated by white spot syndrome virus E3 ubiquitin-
CC protein ligase WSSV222. This targets the protein for rapid degradation
CC via the ubiquitin system. {ECO:0000269|PubMed:16571805}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY683323; AAU13908.1; -; mRNA.
DR AlphaFoldDB; Q3T7C9; -.
DR SMR; Q3T7C9; -.
DR UniPathway; UPA00559; -.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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 InterPro; IPR035435; DPH1/DPH2_euk_archaea.
DR PANTHER; PTHR10762; PTHR10762; 1.
DR Pfam; PF01866; Diphthamide_syn; 1.
DR PIRSF; PIRSF004967; DPH1; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR TIGRFAMs; TIGR00322; diphth2_R; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Iron; Iron-sulfur; Metal-binding; S-adenosyl-L-methionine;
KW Transferase; Ubl conjugation.
FT CHAIN 1..423
FT /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT subunit 1"
FT /id="PRO_0000410893"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT BINDING 215
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
FT BINDING 342
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:O58832"
SQ SEQUENCE 423 AA; 47024 MW; 8C86E04C94088F23 CRC64;
MNMEEDTQSK EIVVAPKKEK KVFRPARSVI KGVPAEIEKD PKLQKAIEVL PSNYNFEIPK
TIWRVKQANA KHVALQFPEG LLLFATSIAD IIETWTEAET TIMGDVTYGA CCVDDFTARA
VGADFMVHYG HSCLVPIDQT GSIPCLYVFV DIQFDTVHLI DTIKSVFPST VPLALVSIIQ
FVSSLQKMAQ DLKSCGYTVC VPQCRPLSPG EVLGCTSPPV PEGHTIVCLG DGRFHLESIM
ISNPEVPTYL YNPYSKVLSR EYYDQPLMKK IRKEIIDKAS TAKKWGLILG TLGRQGNTKV
MENLKNQLEA AGKDFVIVLL SEIFPAKLEA MSDVEAWVQV ACPRLSIDWG ASFPRPLLNP
YEATVALKHA EWHAQRYPMD FYANESLGEW TPNHKPPCPC GQTRNTGCKG LRCPSSKQGS
NKD
