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 26-NOV-2014, entry version 70. 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; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15238247; RA West C.M., Van Der Wel H., Sassi S., Gaucher E.A.; RT "Cytoplasmic glycosylation of protein-hydroxyproline and its RT relationship 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., RA Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., RA Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., RA Platzer M., Rosenthal A., 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., RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., RA 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., RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., RA Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). RN [4] RP FUNCTION, AND ENZYME REGULATION. RX PubMed=11358877; DOI=10.1093/glycob/11.4.283; RA Sassi S., Sweetinburgh M., Erogul J., Zhang P., Teng-Umnuay P., RA West C.M.; RT "Analysis of Skp1 glycosylation and nuclear enrichment in RT 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 RT hypoxia-inducible factor-alpha class of animal prolyl 4- RT 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: Peptide L-proline + 2-oxoglutarate + O(2) = CC Peptide 4-hydroxy-L-proline + succinate + CO(2). CC {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 -!- ENZYME 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 CC (the 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 -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00805}. 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 ProteinModelPortal; Q86KR9; -. DR BioGrid; 1246210; 1. DR STRING; 44689.DDB_0231040; -. DR EnsemblProtists; DDB0231040; DDB0231040; DDB_G0277759. DR GeneID; 8621207; -. DR KEGG; ddi:DDB_G0277759; -. DR dictyBase; DDB_G0277759; phyA. DR eggNOG; COG3751; -. DR InParanoid; Q86KR9; -. DR OMA; FYHELNT; -. DR PhylomeDB; Q86KR9; -. DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. 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: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 InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase. DR InterPro; IPR006620; Pro_4_hyd_alph. 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 Complete proteome; Cytoplasm; Dioxygenase; Iron; Metal-binding; KW Oxidoreductase; Reference proteome; Vitamin C. FT CHAIN 1 284 Prolyl 4-hydroxylase subunit alpha. FT /FTId=PRO_0000327577. FT DOMAIN 169 284 Fe2OG dioxygenase. {ECO:0000255|PROSITE- FT ProRule:PRU00805}. FT COMPBIAS 24 40 Asn-rich. FT COMPBIAS 28 31 Poly-Ser. FT METAL 191 191 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00805}. FT METAL 193 193 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00805}. FT METAL 266 266 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00805}. FT BINDING 276 276 2-oxoglutarate. {ECO:0000255|PROSITE- FT ProRule:PRU00805}. 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 //