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Database: UniProt
Entry: G3B3F1_CANTC
LinkDB: G3B3F1_CANTC
Original site: G3B3F1_CANTC 
ID   G3B3F1_CANTC            Unreviewed;       416 AA.
AC   G3B3F1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, 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, ECO:0000256|PIRNR:PIRNR004967};
DE            EC=2.5.1.108 {ECO:0000256|ARBA:ARBA00012221, ECO:0000256|PIRNR:PIRNR004967};
GN   ORFNames=CANTEDRAFT_114183 {ECO:0000313|EMBL:EGV64386.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV64386.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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   -!- SUBUNIT: Component of the 2-(3-amino-3-carboxypropyl)histidine synthase
CC       complex composed of DPH1, DPH2, DPH3 and a NADH-dependent reductase,
CC       predominantly CBR1. {ECO:0000256|ARBA:ARBA00034128}.
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; GL996521; EGV64386.1; -; Genomic_DNA.
DR   RefSeq; XP_006686700.1; XM_006686637.1.
DR   AlphaFoldDB; G3B3F1; -.
DR   STRING; 590646.G3B3F1; -.
DR   GeneID; 18247305; -.
DR   eggNOG; KOG2648; Eukaryota.
DR   HOGENOM; CLU_037146_1_1_1; -.
DR   OrthoDB; 5472575at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000000707; 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   Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR004967};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004967}.
SQ   SEQUENCE   416 AA;  47159 MW;  D78EE05445D41995 CRC64;
     MVEPTQEVAT TTPVKEKRRF VGRKATPADG KSLVKTSRSK VISRVMNQIP EDILNNKDLN
     QAIKLLPSNY NFEIHKTVWN IRKNNAKRVA LQLPEGLLIY SLVISDILEQ FCEVETVVMG
     DVTYGACCID DYTAKALDCD FIVHYAHSCL VPVDVTSIKV LYIFVTIHID EKHLINTIKL
     NFTAGTNLAV FGTIQFNPTI HSVKAKLEHD EEHPVYLIPP QLKPLSKGEV LGCTSQRLDK
     NHIQGMVYVG DGRFHLESSM IHNPDIPAFR YDPYSRKFTR EYYDQEQMVQ VREDAITVAK
     NAKTVGLILG GLGRQGNPVT VGNLEVKLVQ YGYKVVRIIL SEIFPQKLAM FNDIDAFIQV
     ACPRLSIDWG YAFNKPLLTP YEAMVMMEAD KKWDTFYPMD YYALDGYGRG KQPARS
//
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