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Database: UniProt
Entry: G2WHK1_YEASK
LinkDB: G2WHK1_YEASK
Original site: G2WHK1_YEASK 
ID   G2WHK1_YEASK            Unreviewed;       534 AA.
AC   G2WHK1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000256|RuleBase:RU364133};
GN   Name=K7_DPH2 {ECO:0000313|EMBL:GAA24544.1};
GN   ORFNames=SYK7_041411 {ECO:0000313|EMBL:GAA24544.1};
OS   Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's
OS   yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=721032 {ECO:0000313|EMBL:GAA24544.1, ECO:0000313|Proteomes:UP000001608};
RN   [1] {ECO:0000313|EMBL:GAA24544.1, ECO:0000313|Proteomes:UP000001608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608};
RX   PubMed=21900213; DOI=10.1093/dnares/dsr029;
RA   Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D.,
RA   Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S.,
RA   Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T.,
RA   Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A.,
RA   Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A.,
RA   Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.;
RT   "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no.
RT   7.";
RL   DNA Res. 18:423-434(2011).
CC   -!- FUNCTION: Required for the first step of diphthamide biosynthesis, a
CC       post-translational modification of histidine which occurs in elongation
CC       factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group
CC       from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction
CC       is assisted by a reduction system comprising DPH3 and a NADH-dependent
CC       reductase. Facilitates the reduction of the catalytic iron-sulfur
CC       cluster found in the DPH1 subunit. {ECO:0000256|RuleBase:RU364133}.
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, ECO:0000256|RuleBase:RU364133}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364133}.
CC   -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006179, ECO:0000256|RuleBase:RU364133}.
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DR   EMBL; DG000047; GAA24544.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2WHK1; -.
DR   HOGENOM; CLU_015210_1_0_1; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000001608; Chromosome XI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-EC.
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; 3.40.50.11860; Diphthamide synthesis DPH1/DPH2 domain 3; 1.
DR   InterPro; IPR010014; DHP2.
DR   InterPro; IPR016435; DPH1/DPH2.
DR   InterPro; IPR042263; DPH1/DPH2_1.
DR   InterPro; IPR042265; DPH1/DPH2_3.
DR   NCBIfam; TIGR00322; diphth2_R; 1.
DR   NCBIfam; TIGR00272; DPH2; 1.
DR   PANTHER; PTHR10762:SF2; 2-(3-AMINO-3-CARBOXYPROPYL)HISTIDINE SYNTHASE SUBUNIT 2; 1.
DR   PANTHER; PTHR10762; DIPHTHAMIDE BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF01866; Diphthamide_syn; 1.
DR   SFLD; SFLDG01121; Diphthamide_biosynthesis; 1.
DR   SFLD; SFLDF00408; Diphthamide_biosynthesis_famil; 1.
DR   SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU364133};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364133};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364133};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364133}.
SQ   SEQUENCE   534 AA;  59794 MW;  DBE401CA37652FAD CRC64;
     MEVAPALSTT QSDVAFQKVE THEIDRSSYL GPCYNSDELM QLISAYYNVE PLVGYLEQHP
     EYQNVTLQFP DDLIKDSSLI VRLLQSKFPH GKIKFWVLAD TAYSACCVDE VAAEHVRAEV
     VVHFGDACLN AIQNLPVVYS FGTPFLDLAL VVENFQRAFP DLSSKICLMA NAPFSKHLSQ
     LYNILKGDLH YTNIIYSQVN TSAVEEKFVT ILDTFHVPED VDQVGVFEKN SVLFGQHDKA
     DNISPEDYHL FHLTTPQDPR LLYLSTVFQS VHIFDPALPG MVTGPFPSLM RRYKYMHVAR
     TAGCIGILVN TLSLRNTRET INELVKLIKT REKKHYLFVV GKPNVAKLAN FEDIDIWCIL
     GCSQSGIIVD QFNEFYKPII TPYELNLALS EEVTWTGKWV VDFRDAIDEI EQNLGGQDTI
     SASTTSDEPE FDVVRGRYTS TSRPLRALTH LELEAADDDD SKQLTTRHTA SGAVIKGTVS
     TSASALQNRS WKGLGSDFDS TEVDNTGADI EEGISGVARG YGFDREDAMK KENK
//
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