ID B0XSX2_ASPFC Unreviewed; 445 AA.
AC B0XSX2;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000256|ARBA:ARBA00021915, ECO:0000256|PIRNR:PIRNR004967};
DE EC=2.5.1.108 {ECO:0000256|ARBA:ARBA00012221, ECO:0000256|PIRNR:PIRNR004967};
GN ORFNames=AFUB_028100 {ECO:0000313|EMBL:EDP54750.1};
OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP54750.1, ECO:0000313|Proteomes:UP000001699};
RN [1] {ECO:0000313|EMBL:EDP54750.1, ECO:0000313|Proteomes:UP000001699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC {ECO:0000313|Proteomes:UP000001699};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- FUNCTION: Catalyzes the first step of diphthamide biosynthesis, a post-
CC translational modification of histidine which occurs in elongation
CC factor 2. {ECO:0000256|PIRNR:PIRNR004967}.
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 ECO:0000256|PIRNR:PIRNR004967};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRNR:PIRNR004967};
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:0000256|PIRNR:PIRNR004967};
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156, ECO:0000256|PIRNR:PIRNR004967}.
CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC {ECO:0000256|ARBA:ARBA00010173, ECO:0000256|PIRNR:PIRNR004967}.
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DR EMBL; DS499595; EDP54750.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XSX2; -.
DR SMR; B0XSX2; -.
DR EnsemblFungi; EDP54750; EDP54750; AFUB_028100.
DR VEuPathDB; FungiDB:AFUB_028100; -.
DR HOGENOM; CLU_037146_1_1_1; -.
DR PhylomeDB; B0XSX2; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniRule.
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 InterPro; IPR035435; DPH1/DPH2_euk_archaea.
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 PIRSF; PIRSF004967; DPH1; 1.
DR SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|PIRNR:PIRNR004967};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR004967};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004967}.
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 445 AA; 49244 MW; 03287B6637F3BF28 CRC64;
MTEPLLSSAA PEMKMEETSS SSNLRQPKKR FVGRRTADAH AQKDASISSK DVESTSVQRV
APRRNPRTLN QVPPEILDDP EIQAAIELLP KNYSFEIPKT IHRIRTSGAK RVALQFPEGL
LIFATTISDI LTQFCPGTET LIMGDVTYGA CCIDDYTARA LGCDLLVHYA HSCLIPVDVT
QIKTLYIFVD ISIDTSHLIA TLERNFQPGK TIATVGTIQF NATLHGLKPV LERAGFKVVI
PQIAPLSKGE ILGCTSPQLS PTEIDILLYL GDGRFHLESA MIHNPTIPAY RYDPYSRTLS
RETYSHDEMH ALRRDAINTA KSAKKWGIIL GSLGRQGNPN TMAMIENHLN ERGIPFVNLL
LSEIFPGKLA SMSDVECWVQ IACPRLSIDW GYAFPRPLLT PYEALIALGV REHWDSANSG
VYPMDFYAKE GLGRTKPQQA LQGAA
//
