ID X0V5W6_9ZZZZ Unreviewed; 271 AA.
AC X0V5W6;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase {ECO:0000256|ARBA:ARBA00012221};
DE EC=2.5.1.108 {ECO:0000256|ARBA:ARBA00012221};
DE Flags: Fragment;
GN ORFNames=S01H1_34831 {ECO:0000313|EMBL:GAG06787.1};
OS marine sediment metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=412755 {ECO:0000313|EMBL:GAG06787.1};
RN [1] {ECO:0000313|EMBL:GAG06787.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAG06787.1};
RX PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA Takami H.;
RT "High frequency of phylogenetically diverse reductive dehalogenase-
RT homologous genes in deep subseafloor sedimentary metagenomes.";
RL Front. Microbiol. 5:80-80(2014).
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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAG06787.1}.
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DR EMBL; BARS01021715; GAG06787.1; -; Genomic_DNA.
DR AlphaFoldDB; X0V5W6; -.
DR UniPathway; UPA00559; -.
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; 3.40.50.11850; 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 InterPro; IPR022428; Dph2_arc.
DR NCBIfam; TIGR03682; arCOG04112; 1.
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 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:GAG06787.1"
FT NON_TER 271
FT /evidence="ECO:0000313|EMBL:GAG06787.1"
SQ SEQUENCE 271 AA; 30020 MW; F79F597C546AFB81 CRC64;
KVVLENGYKT VALQVPEGLK RSVWNVVEFL EKKTQAKIIV IADPCFGACD LVNYELKNLD
VDFVIHIGHT SIPDVENFWI PTLFINAVST KDVSAVVERS LSSLEGKKIG IVTTAQHLHT
LEVVDRILKK HDFVPIISDG DERISEKGQI LGCNFSAGMN IVDKVDSFLF VGSGNFHPVG
LLLSSKKPVI AADPYTNTVK KQELDDLKDT ILRQRYGAIA NSKNAKKFGI LVGIKRGQQR
VELADEIKEM LDSFNKKSMI IALDNFSPVS L
//
