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DOHH_DICDI
ID   DOHH_DICDI              Reviewed;         315 AA.
AC   Q556G4; Q86K26;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Deoxyhypusine hydroxylase {ECO:0000255|HAMAP-Rule:MF_03101};
DE            Short=DOHH {ECO:0000255|HAMAP-Rule:MF_03101};
DE            EC=1.14.99.29 {ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine dioxygenase {ECO:0000255|HAMAP-Rule:MF_03101};
DE   AltName: Full=Deoxyhypusine monooxygenase {ECO:0000255|HAMAP-Rule:MF_03101};
GN   Name=dohh-1; ORFNames=DDB_G0272634;
GN   and
GN   Name=dohh-2; ORFNames=DDB_G0274079;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-
CC       lysine intermediate produced by deoxyhypusine synthase/DHPS on a
CC       critical lysine of the eukaryotic translation initiation factor 5A/eIF-
CC       5A. This is the second step of the post-translational modification of
CC       that lysine into an unusual amino acid residue named hypusine.
CC       Hypusination is unique to mature eIF-5A factor and is essential for its
CC       function. {ECO:0000250|UniProtKB:Q99LN9, ECO:0000255|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:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
CC         Rule:MF_03101};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q9BU89,
CC         ECO:0000255|HAMAP-Rule:MF_03101};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9BU89,
CC       ECO:0000255|HAMAP-Rule:MF_03101};
CC   -!- PATHWAY: Protein modification; eIF5A hypusination.
CC       {ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-Rule:MF_03101}.
CC   -!- SIMILARITY: Belongs to the deoxyhypusine hydroxylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03101}.
CC   -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC       AX4. These strains contain a duplication of a segment of 750 kb of
CC       chromosome 2 compared to the corresponding sequence in strain AX2.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000009; EAL70954.1; -; Genomic_DNA.
DR   EMBL; AAFI02000011; EAL70473.1; -; Genomic_DNA.
DR   RefSeq; XP_644398.1; XM_639306.1.
DR   RefSeq; XP_645015.1; XM_639923.1.
DR   AlphaFoldDB; Q556G4; -.
DR   SMR; Q556G4; -.
DR   STRING; 44689.DDB0233909; -.
DR   PaxDb; Q556G4; -.
DR   EnsemblProtists; EAL70473; EAL70473; DDB_G0274079.
DR   EnsemblProtists; EAL70954; EAL70954; DDB_G0272634.
DR   GeneID; 8618692; -.
DR   GeneID; 8619284; -.
DR   KEGG; ddi:DDB_G0272634; -.
DR   KEGG; ddi:DDB_G0274079; -.
DR   dictyBase; DDB_G0272634; dohh-1.
DR   dictyBase; DDB_G0274079; dohh-2.
DR   eggNOG; KOG0567; Eukaryota.
DR   HOGENOM; CLU_053974_0_0_1; -.
DR   InParanoid; Q556G4; -.
DR   OMA; MEPNCSA; -.
DR   PhylomeDB; Q556G4; -.
DR   Reactome; R-DDI-204626; Hypusine synthesis from eIF5A-lysine.
DR   UniPathway; UPA00354; -.
DR   PRO; PR:Q556G4; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0019135; F:deoxyhypusine monooxygenase activity; ISS:dictyBase.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; ISS:dictyBase.
DR   Gene3D; 1.25.10.10; -; 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   SMART; SM00567; EZ_HEAT; 6.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Hypusine biosynthesis; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Repeat.
FT   CHAIN           1..315
FT                   /note="Deoxyhypusine hydroxylase"
FT                   /id="PRO_0000326491"
FT   REPEAT          23..52
FT                   /note="HEAT-like PBS-type 1"
FT   REPEAT          56..82
FT                   /note="HEAT-like PBS-type 2"
FT   REPEAT          89..115
FT                   /note="HEAT-like PBS-type 3"
FT   REPEAT          179..205
FT                   /note="HEAT-like PBS-type 4"
FT   REPEAT          211..237
FT                   /note="HEAT-like PBS-type 5"
FT   REPEAT          244..270
FT                   /note="HEAT-like PBS-type 6"
FT   BINDING         58
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
FT   BINDING         91
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
FT   BINDING         92
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
FT   BINDING         213
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
FT   BINDING         246
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
FT   BINDING         247
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BU89, ECO:0000255|HAMAP-
FT                   Rule:MF_03101"
SQ   SEQUENCE   315 AA;  35241 MW;  E798E6365097DFFE CRC64;
     MVVVTEEIVN GLKETLTDVS QPIAKRFRSL FTLRNLNGPL CIDAMASALN DKSALLRHEI
     AYCLGQMEDE YALKVLIDLV KNSDEHPMVR HEAAEALGAI GSESAHKTLK EYSNDPVREV
     SETCQLALSR VEWYEKNKPE TEEDKMYMSV DPAPPLKKGS VSRDELRSKF LDSNLDIFNR
     YRALFSLRDI GDEQSVLALC DGLKDQSSAL LRHEVAFVLG QLQHRVAIDP LTTCVLDESE
     NAMVRHEAAE ALGAIASTET IPLLEKLLQD KEPIVSESCA VALDVTEYFN NTESFQYADG
     IKILLEKNLV DQQQK
 
 
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