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Database: UniProt
Entry: A0A103XP55_CYNCS
LinkDB: A0A103XP55_CYNCS
Original site: A0A103XP55_CYNCS 
ID   A0A103XP55_CYNCS        Unreviewed;       349 AA.
AC   A0A103XP55;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Deoxyhypusine hydroxylase {ECO:0000256|HAMAP-Rule:MF_03101};
DE            Short=DOHH {ECO:0000256|HAMAP-Rule:MF_03101};
DE            EC=1.14.99.29 {ECO:0000256|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine dioxygenase {ECO:0000256|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine monooxygenase {ECO:0000256|HAMAP-Rule:MF_03101};
GN   ORFNames=Ccrd_003621 {ECO:0000313|EMBL:KVH94265.1};
OS   Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC   Carduinae; Cynara.
OX   NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH94265.1, ECO:0000313|Proteomes:UP000243975};
RN   [1] {ECO:0000313|EMBL:KVH94265.1, ECO:0000313|Proteomes:UP000243975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2C {ECO:0000313|EMBL:KVH94265.1};
RX   PubMed=26786968; DOI=10.1038/srep19427;
RA   Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA   Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA   Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT   "The genome sequence of the outbreeding globe artichoke constructed de novo
RT   incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL   Sci. Rep. 6:19427-19427(2016).
CC   -!- FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-
CC       lysine intermediate to form hypusine, an essential post-translational
CC       modification only found in mature eIF-5A factor. {ECO:0000256|HAMAP-
CC       Rule:MF_03101}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[eIF5A protein]-deoxyhypusine + AH2 + O2 = [eIF5A protein]-
CC         hypusine + A + H2O; Xref=Rhea:RHEA:14101, Rhea:RHEA-COMP:10144,
CC         Rhea:RHEA-COMP:12592, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:82657,
CC         ChEBI:CHEBI:91175; EC=1.14.99.29;
CC         Evidence={ECO:0000256|ARBA:ARBA00000068, ECO:0000256|HAMAP-
CC         Rule:MF_03101};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03101};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03101};
CC   -!- PATHWAY: Protein modification; eIF5A hypusination.
CC       {ECO:0000256|ARBA:ARBA00005041, ECO:0000256|HAMAP-Rule:MF_03101}.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03101}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03101}.
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:KVH94265.1}.
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DR   EMBL; LEKV01004559; KVH94265.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A103XP55; -.
DR   STRING; 59895.A0A103XP55; -.
DR   EnsemblPlants; KVH94265; KVH94265; Ccrd_003621.
DR   Gramene; KVH94265; KVH94265; Ccrd_003621.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000243975; Unassembled WGS sequence.
DR   GO; GO:0019135; F:deoxyhypusine monooxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   HAMAP; MF_03101; Deoxyhypusine_hydroxylase; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR027517; Deoxyhypusine_hydroxylase.
DR   InterPro; IPR004155; PBS_lyase_HEAT.
DR   PANTHER; PTHR12697:SF5; DEOXYHYPUSINE HYDROXYLASE; 1.
DR   PANTHER; PTHR12697; PBS LYASE HEAT-LIKE PROTEIN; 1.
DR   Pfam; PF13646; HEAT_2; 1.
DR   Pfam; PF03130; HEAT_PBS; 1.
DR   SMART; SM00567; EZ_HEAT; 5.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Hypusine biosynthesis {ECO:0000256|ARBA:ARBA00023256, ECO:0000256|HAMAP-
KW   Rule:MF_03101};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03101};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_03101};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW   Rule:MF_03101};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_03101}; Reference proteome {ECO:0000313|Proteomes:UP000243975}.
FT   BINDING         85
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         117
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         118
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         253
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         254
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         286
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         287
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
SQ   SEQUENCE   349 AA;  38636 MW;  4B4266D91FD5019C CRC64;
     MLSRSIWPNT LNSLQKLGFW QFDLSTLPPF FLKLQALSSS WKWRLMEIRS KSLLRQRNFF
     ASDYWTKRNR FRSGSESSSL SGICEAAFAL GQMQDADAIP ALKLVLNDLS LHPIVRHEVD
     FSPALAFFPF AAEALGAIGL ESNIPLLKDS LDSDPAQEVR ETCELALSRI QELKNAGDNH
     QSSTTAASPF LSVDPAAPAS CSSVHKLREV ILNEEKGMYE RYGALFGLRN HGGDEAVAAV
     IESLNAKSAL LRHEVAYVLG QLQNKSASDA LSRILKDVNE HPMVRHEAAE ALGSIADDQC
     ISLLEEFSKD PEPIVSQSCE VALSMLDFER SGKSFEYLFM QAPQLQEAT
//
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