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Database: UniProt
Entry: L9KHJ4_TUPCH
LinkDB: L9KHJ4_TUPCH
Original site: L9KHJ4_TUPCH 
ID   L9KHJ4_TUPCH            Unreviewed;       490 AA.
AC   L9KHJ4;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000256|ARBA:ARBA00021914, ECO:0000256|RuleBase:RU364133};
GN   ORFNames=TREES_T100004227 {ECO:0000313|EMBL:ELW62143.1};
OS   Tupaia chinensis (Chinese tree shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX   NCBI_TaxID=246437 {ECO:0000313|EMBL:ELW62143.1, ECO:0000313|Proteomes:UP000011518};
RN   [1] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhang G., Fan Y., Yao Y., Huang Z.;
RT   "Genome of the Chinese tree shrew, a rising model animal genetically
RT   related to primates.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000011518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23385571; DOI=10.1038/ncomms2416;
RA   Fan Y., Huang Z.Y., Cao C.C., Chen C.S., Chen Y.X., Fan D.D., He J.,
RA   Hou H.L., Hu L., Hu X.T., Jiang X.T., Lai R., Lang Y.S., Liang B.,
RA   Liao S.G., Mu D., Ma Y.Y., Niu Y.Y., Sun X.Q., Xia J.Q., Xiao J.,
RA   Xiong Z.Q., Xu L., Yang L., Zhang Y., Zhao W., Zhao X.D., Zheng Y.T.,
RA   Zhou J.M., Zhu Y.B., Zhang G.J., Wang J., Yao Y.G.;
RT   "Genome of the Chinese tree shrew.";
RL   Nat. Commun. 4:1426-1426(2013).
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   -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00006179, ECO:0000256|RuleBase:RU364133}.
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DR   EMBL; KB320836; ELW62143.1; -; Genomic_DNA.
DR   RefSeq; XP_006153825.1; XM_006153763.2.
DR   AlphaFoldDB; L9KHJ4; -.
DR   STRING; 246437.L9KHJ4; -.
DR   GeneID; 102488549; -.
DR   KEGG; tup:102488549; -.
DR   CTD; 1802; -.
DR   eggNOG; KOG2648; Eukaryota.
DR   InParanoid; L9KHJ4; -.
DR   OrthoDB; 5491765at2759; -.
DR   UniPathway; UPA00559; -.
DR   Proteomes; UP000011518; Unassembled WGS sequence.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011518}.
SQ   SEQUENCE   490 AA;  52644 MW;  FF5EF586A7B0913B CRC64;
     MESTFSSPAE AALQREAGVL GPRTPLADLD RVYELERVVG FVRDLGCHRV ALQFPDQLLG
     DARAVAARLE ETTGSKMFIL GDTAYGSCCV DVLGAEQAGA QALVHFGPAC LSPPARPLPV
     TFVFGHRSVT LELCAKAFET QNPDPTAPVV LLSEPACAHA LEALATRLRP RYLDLLVSRP
     ALPLPEGSLD SEPETVERFG RRFPLAPGRH LEEYGAFYVG DSEASSDSDL EPDLSRLLLG
     WAPGQPFFSC CPDTGRTRDE SARAGRLRAR RHYLVERARD AHVVGLLAGT LGVAQHREAL
     AHLRKLTRAS GKRSYVLALG RPTPAKLANF PEVDVFVLLA CPLGTLAPQP SGGFFRPILG
     PCELEAACNP AWPPAGLAPH LTHYVDLLPG SPFHVPLPPP ESELWDTPDV SLISGELRLP
     AAWKLSGDPV CSSALNPRPQ LELAESSPAA SFLTSRSWQG LEPRLGQTPV TDAITGRRGI
     AIAYEDEGNS
//
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