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DPH1_CANAL
ID   DPH1_CANAL              Reviewed;         426 AA.
AC   Q59MG1; A0A1D8PHJ2; Q59MG0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 3.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 {ECO:0000305};
DE            EC=2.5.1.108 {ECO:0000250|UniProtKB:P40487};
DE   AltName: Full=Diphthamide biosynthesis protein 1;
DE   AltName: Full=Diphtheria toxin resistance protein 1 {ECO:0000305};
DE   AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1 {ECO:0000305};
GN   Name=DPH1; OrderedLocusNames=CAALFM_C205840WA;
GN   ORFNames=CaO19.12674/12675, CaO19.5207/5208;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- FUNCTION: Catalyzes the first step of diphthamide biosynthesis, a post-
CC       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, predominantly CBR1. {ECO:0000250|UniProtKB:P40487}.
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:0000250|UniProtKB:P40487};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P40487};
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:0000250|UniProtKB:P40487};
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
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:0000250|UniProtKB:P40487}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P40487}.
CC   -!- SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP017624; AOW27595.1; -; Genomic_DNA.
DR   RefSeq; XP_710915.2; XM_705823.2.
DR   AlphaFoldDB; Q59MG1; -.
DR   SMR; Q59MG1; -.
DR   STRING; 237561.Q59MG1; -.
DR   GeneID; 3647484; -.
DR   KEGG; cal:CAALFM_C205840WA; -.
DR   CGD; CAL0000187558; orf19.12674.
DR   VEuPathDB; FungiDB:C2_05840W_A; -.
DR   eggNOG; KOG2648; Eukaryota.
DR   HOGENOM; CLU_112098_0_0_1; -.
DR   InParanoid; Q59MG1; -.
DR   OMA; PGQVLGC; -.
DR   OrthoDB; 750182at2759; -.
DR   UniPathway; UPA00559; -.
DR   PRO; PR:Q59MG1; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR   GO; GO:0090560; F:2-(3-amino-3-carboxypropyl)histidine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB.
DR   GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; ISS:UniProtKB.
DR   Gene3D; 3.40.50.11840; -; 1.
DR   Gene3D; 3.40.50.11850; -; 1.
DR   Gene3D; 3.40.50.11860; -; 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   PANTHER; PTHR10762; PTHR10762; 1.
DR   Pfam; PF01866; Diphthamide_syn; 1.
DR   PIRSF; PIRSF004967; DPH1; 1.
DR   SFLD; SFLDS00032; Radical_SAM_3-amino-3-carboxyp; 1.
DR   TIGRFAMs; TIGR00322; diphth2_R; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Iron; Iron-sulfur; Metal-binding; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..426
FT                   /note="2-(3-amino-3-carboxypropyl)histidine synthase
FT                   subunit 1"
FT                   /id="PRO_0000083369"
FT   BINDING         132
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O58832"
FT   BINDING         238
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O58832"
FT   BINDING         367
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:O58832"
SQ   SEQUENCE   426 AA;  48532 MW;  CB83F0C71E371E3E CRC64;
     MSPVEKPVEV EKPKVPKRRF VGKKPQNITI KDGEQPLTKT INPARHIGRV MNQIPDDILN
     DKELNEAIKL LPSNYNFEIH KTIWNIRKTN CKRVALQMPE GLLIYSLIIS DILEQFCQVE
     TIVMGDVSYG ACCIDDYTAR SLDCDFIVHY AHSCLVPIDI TSIKVLYVFV TINIDETHLI
     NTIKLNFERG TQIAIFGTIQ FNPTIHSVKA KLENDTEKPM YLIPPQTRPL SKGEVLGCTS
     ARLDKEHIKA MIYIGDGRFH LESSMIHNPE IPAYRYDPYS RKFTREYYDH KQMIDVRKDA
     ISTTKYATKV GLILGALGRQ GNPITLDKLE KSLSEKGIQV VKIILSEILP QKLAMFDDVD
     AFVQVACPRL SIDWGYAFNK PLLTPYEAMV MLEKDTMGDE KVYPMDYYSK DGYGRGSIPD
     HSHLTT
 
 
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