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Database: UniProt
Entry: B8NNR3_ASPFN
LinkDB: B8NNR3_ASPFN
Original site: B8NNR3_ASPFN 
ID   B8NNR3_ASPFN            Unreviewed;       339 AA.
AC   B8NNR3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-NOV-2023, entry version 88.
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   Name=LIA1 {ECO:0000256|HAMAP-Rule:MF_03101};
GN   ORFNames=AFLA_129640 {ECO:0000313|EMBL:EED48741.1}, G4B84_002724
GN   {ECO:0000313|EMBL:QMW27435.1};
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952 {ECO:0000313|EMBL:EED48741.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED48741.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000001875}, and NRRL3357
RC   {ECO:0000313|EMBL:EED48741.1};
RX   PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
RN   [2] {ECO:0000313|EMBL:QMW27435.1, ECO:0000313|Proteomes:UP000515286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL3357 {ECO:0000313|EMBL:QMW27435.1,
RC   ECO:0000313|Proteomes:UP000515286};
RA   Fountain J.C., Clevenger J.P., Nadon B., Youngblood R.C., Korani W.,
RA   Chang P.-K., Starr D., Wang H., Isett B., Johnston H.R., Wiggins R.,
RA   Chu Y., Agarwal G., Kemerait R.C., Pandey M.K., Bhatnagar D.,
RA   Ozias-Akins P., Varshney R.K., Scheffler B.E., Vaughn J.N., Guo B.;
RT   "Two New Chromosome-Level Aspergillus flavus Reference Genomes Reveal a
RT   Large Insertion Potentially Contributing to Isolate Stress Tolerance and
RT   Aflatoxin Production.";
RL   Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03101}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03101}.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03101}.
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DR   EMBL; EQ963481; EED48741.1; -; Genomic_DNA.
DR   EMBL; CP059867; QMW27435.1; -; Genomic_DNA.
DR   RefSeq; XP_002382157.1; XM_002382116.1.
DR   AlphaFoldDB; B8NNR3; -.
DR   SMR; B8NNR3; -.
DR   STRING; 332952.B8NNR3; -.
DR   EnsemblFungi; EED48741; EED48741; AFLA_129640.
DR   VEuPathDB; FungiDB:AFLA_012793; -.
DR   eggNOG; KOG0567; Eukaryota.
DR   HOGENOM; CLU_053974_0_0_1; -.
DR   OMA; GQLQEPC; -.
DR   OrthoDB; 5474306at2759; -.
DR   UniPathway; UPA00354; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   Proteomes; UP000515286; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; IPR021133; HEAT_type_2.
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; 2.
DR   SMART; SM00567; EZ_HEAT; 5.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03101};
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}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03101};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_03101}.
FT   REPEAT          254..294
FT                   /note="HEAT"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT   REGION          159..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         73
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         74
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         106
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         107
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         240
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         241
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         273
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
FT   BINDING         274
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03101"
SQ   SEQUENCE   339 AA;  36986 MW;  D7CF8BAA0F916D3D CRC64;
     MASSAVDQPE GVDETILTLR KVLVNESEPL ARRFRALFSL KYIACLQPPT EKTLPAIQAI
     AAGFTSSSAL LKHELAYCLG QTRNPDAVSY LLEVVKNTEQ DAMCRHEAAE GLGALGFDTS
     LDVLKALRDD EKEEDVIRET CDIAVDRILW ENSEERKSEK LKPSDFTSID PAPPLPMASS
     QPSISDLEKT LLDTKLPLFQ RYRAMFALRD LASPPDLPTA VEAVEALAKG LKDPSALFRH
     EVAFVFGQLC HPASVPSLTE TLSDQKEMGM VRHEAAEALG SLGDVEGVED TLKKFLNDPE
     QVVRDSIIVA LDMAEYEKNG EMEYALVPDS AAPAAVSAA
//
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