ID H6CBC7_EXODN Unreviewed; 445 AA.
AC H6CBC7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000256|ARBA:ARBA00021915};
DE EC=2.5.1.108 {ECO:0000256|ARBA:ARBA00012221};
DE AltName: Full=Diphthamide biosynthesis protein 1 {ECO:0000256|ARBA:ARBA00032574};
DE AltName: Full=Diphtheria toxin resistance protein 1 {ECO:0000256|ARBA:ARBA00032789};
DE AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1 {ECO:0000256|ARBA:ARBA00031690};
GN ORFNames=HMPREF1120_09013 {ECO:0000313|EMBL:EHY61074.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY61074.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY61074.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY61074.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001323};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC {ECO:0000256|ARBA:ARBA00010173}.
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DR EMBL; JH226137; EHY61074.1; -; Genomic_DNA.
DR RefSeq; XP_009161535.1; XM_009163287.1.
DR AlphaFoldDB; H6CBC7; -.
DR STRING; 858893.H6CBC7; -.
DR GeneID; 20313652; -.
DR VEuPathDB; FungiDB:HMPREF1120_09013; -.
DR eggNOG; KOG2648; Eukaryota.
DR HOGENOM; CLU_037146_1_1_1; -.
DR InParanoid; H6CBC7; -.
DR OMA; PGQVLGC; -.
DR OrthoDB; 5472575at2759; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.11840; Diphthamide synthesis DPH1/DPH2 domain 1; 1.
DR Gene3D; 3.40.50.11850; Diphthamide synthesis DPH1/DPH2 domain 2; 1.
DR Gene3D; 3.40.50.11860; Diphthamide synthesis DPH1/DPH2 domain 3; 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 NCBIfam; TIGR00322; diphth2_R; 1.
DR PANTHER; PTHR10762:SF1; 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE SUBUNIT 1; 1.
DR PANTHER; PTHR10762; DIPHTHAMIDE BIOSYNTHESIS PROTEIN; 1.
DR Pfam; PF01866; Diphthamide_syn; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 48919 MW; 399855930E4C5D9D CRC64;
MDTEQPAMPG AFPASEDTIS TTRTPKRRFV GRRTAEAQAK QKQHVGSSVE ETNAIVAKSQ
RKTPRALNQI PPEILDDPDI QAAVGLLPHN YSFEIPKTIH RIRTLQAKRV ALQFPEGLLM
FATTISDILT QFCPGTETLI MGDVTYGACC IDDYTARALG CDLLVHYAHS CLIPVSSSKI
ATLYIFVDIS IDTKHLVSTL SRNIPPGKTI AMVSTIQFNS ALHTIRPALE AEGLKLVVPQ
VMPLSKGEVL GCTAPKIGPD AHVDLILYLG DGRFHLEAAM IANPDIPAYR YDPYSRKLTR
ETYSHDEMLD MRSYAINTAK GAKKWGLILG ALGRQGNPHI LTMIENHLNM QGIPYVNLLL
SEIFPGKLAM FEDVECWVQI ACPRLSIDWG YAFPRPLLTP YEALVVLGAI QGWEKEGGTY
PMNYYANNGL GRATEKVAAQ VGVSA
//