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 22-FEB-2023, entry version 101. 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 (Social amoeba). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY. DR PANTHER; PTHR12907; EGL NINE HOMOLOG-RELATED; 1. DR PANTHER; PTHR12907:SF26; PROLYL HYDROXYLASE EGLN3; 1. 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 //