ID W6QBQ1_PENRF Unreviewed; 569 AA.
AC W6QBQ1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase subunit 2 {ECO:0000256|RuleBase:RU364133};
GN Name=dph2 {ECO:0000313|EMBL:CDM33476.1};
GN ORFNames=PROQFM164_S03g000200 {ECO:0000313|EMBL:CDM33476.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM33476.1};
RN [1] {ECO:0000313|EMBL:CDM33476.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM33476.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792017; CDM33476.1; -; Genomic_DNA.
DR AlphaFoldDB; W6QBQ1; -.
DR STRING; 1365484.W6QBQ1; -.
DR OMA; IEGWVVV; -.
DR OrthoDB; 5491765at2759; -.
DR UniPathway; UPA00559; -.
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}.
FT REGION 86..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 62677 MW; 1F6167562BD24574 CRC64;
MGSEMKSAPV LSTADDRILE EINLVATRDP TAPVSDDELS ITYDIERTLK DIRQARYKRI
ALQFPDDMLP DAPRVFQLLS RGLEREEVGT NGTQPSNQTD PSNADTDLAH SITELQVEDK
TEQHSPRLTI LADTSYGTCC VDEVAAEHVD ADVVVHYGRS CLSPTARLPV IHVFTHKDLP
LEPVIRAFKA TYLDPTTKVI IAADVTFSDH VPTVYARLVE EGYSNIYATE VVHEPSSSIP
NRTVPESVRE APETLADWQL FHISDPPTAL MMTLASRVAA IHIYPTNDLS NENVKPLPAS
TTAVLRRRYG TLASLTTVPI WGILINTLSV KNYLHIVEHV KERIAKAGKK SYMFVVGKLN
AAKVANFSEI GGWVVIGCWE SSLVDSKDFW KPVITPFELE LALKNDSDRV WTGAWQSDFQ
AVLDAPAQEV NGNGDDQETS TSTTMSDEDD MSEPESAPPE FDFRTGRYVS HSRPMRDPAP
RASQVDGSST SGPSAARALA RRAKGDLAMI GGAFSPGAEY LRSQRTWKGL GSDFDIRYDE
EDLDDSTLVK EGRKGIARGY TVGDATDKH
//
