P4HA_DICDI
ID P4HA_DICDI Reviewed; 284 AA.
AC Q86KR9; Q54Z57;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Prolyl 4-hydroxylase subunit alpha;
DE Short=Prolyl 4-hydrolase;
DE EC=1.14.11.-;
GN Name=phyA; Synonyms=p4h1; ORFNames=DDB_G0277759;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15238247; DOI=10.1016/j.bbagen.2004.04.007;
RA West C.M., Van Der Wel H., Sassi S., Gaucher E.A.;
RT "Cytoplasmic glycosylation of protein-hydroxyproline and its relationship
RT to other glycosylation pathways.";
RL Biochim. Biophys. Acta 1673:29-44(2004).
RN [2]
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 [3]
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).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=11358877; DOI=10.1093/glycob/11.4.283;
RA Sassi S., Sweetinburgh M., Erogul J., Zhang P., Teng-Umnuay P., West C.M.;
RT "Analysis of Skp1 glycosylation and nuclear enrichment in Dictyostelium.";
RL Glycobiology 11:283-295(2001).
RN [5]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=15705570; DOI=10.1074/jbc.m500600200;
RA van der Wel H., Ercan A., West C.M.;
RT "The Skp1 prolyl hydroxylase from Dictyostelium is related to the hypoxia-
RT inducible factor-alpha class of animal prolyl 4-hydroxylases.";
RL J. Biol. Chem. 280:14645-14655(2005).
CC -!- FUNCTION: Catalyzes the post-translational formation of 4-
CC hydroxyproline. Probably hydroxylates skp1 on Pro-143.
CC {ECO:0000269|PubMed:11358877}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-prolyl-[Skp1 protein] + O2 = CO2 +
CC succinate + trans-4-hydroxy-L-prolyl-[Skp1 protein];
CC Xref=Rhea:RHEA:48936, Rhea:RHEA-COMP:12265, Rhea:RHEA-COMP:12266,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:61965;
CC Evidence={ECO:0000269|PubMed:15705570};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:15705570};
CC -!- ACTIVITY REGULATION: Inhibited by the prolyl-hydroxylase inhibitors
CC alpha,alpha'-dipyridyl and ethyl 3,4-dihydroxybenzoate.
CC {ECO:0000269|PubMed:11358877}.
CC -!- SUBUNIT: Heterotetramer of two alpha-1 chains and two beta chains (the
CC beta chain is the multi-functional PDI). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the P4HA family. {ECO:0000305}.
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DR EMBL; AY768817; AAV37458.1; -; Genomic_DNA.
DR EMBL; AAFI02000022; EAL68553.1; -; Genomic_DNA.
DR RefSeq; XP_642496.1; XM_637404.1.
DR PDB; 6T8M; X-ray; 2.02 A; A/B/C=60-284.
DR PDBsum; 6T8M; -.
DR AlphaFoldDB; Q86KR9; -.
DR SMR; Q86KR9; -.
DR BioGRID; 1246210; 1.
DR STRING; 44689.DDB0231040; -.
DR PaxDb; Q86KR9; -.
DR EnsemblProtists; EAL68553; EAL68553; DDB_G0277759.
DR GeneID; 8621207; -.
DR KEGG; ddi:DDB_G0277759; -.
DR dictyBase; DDB_G0277759; phyA.
DR eggNOG; KOG3710; Eukaryota.
DR HOGENOM; CLU_981514_0_0_1; -.
DR InParanoid; Q86KR9; -.
DR OMA; FEPRIAI; -.
DR PhylomeDB; Q86KR9; -.
DR BRENDA; 1.14.11.2; 1939.
DR PRO; PR:Q86KR9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0031545; F:peptidyl-proline 4-dioxygenase activity; IDA:dictyBase.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IBA:GO_Central.
DR GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0072592; P:oxygen metabolic process; IMP:dictyBase.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; IDA:dictyBase.
DR GO; GO:0010265; P:SCF complex assembly; IDA:dictyBase.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..284
FT /note="Prolyl 4-hydroxylase subunit alpha"
FT /id="PRO_0000327577"
FT DOMAIN 169..284
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 191
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 193
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 276
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6T8M"
FT HELIX 85..100
FT /evidence="ECO:0007829|PDB:6T8M"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:6T8M"
FT HELIX 147..166
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:6T8M"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:6T8M"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:6T8M"
SQ SEQUENCE 284 AA; 33348 MW; 19AE1D748793D0E3 CRC64;
MDISNLPPHI RQQILGLISK PQQNNDESSS SNNKNNLINN EKVSNVLIDL TSNLKIENFK
IFNKESLNQL EKKGYLIIDN FLNDLNKINL IYDESYNQFK ENKLIEAGMN KGTDKWKDKS
IRGDYIQWIH RDSNSRIQDK DLSSTIRNIN YLLDKLDLIK NEFDNVIPNF NSIKTQTQLA
VYLNGGRYIK HRDSFYSSES LTISRRITMI YYVNKDWKKG DGGELRLYTN NPNNTNQKEL
KQTEEFIDIE PIADRLLIFL SPFLEHEVLQ CNFEPRIAIT TWIY
