ID ERR1_YEAST Reviewed; 437 AA. AC Q12007; Q7LGJ4; DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-JUN-2009, entry version 72. DE RecName: Full=Enolase-related protein 1/2; DE EC=4.2.1.11; DE AltName: Full=2-phosphoglycerate dehydratase; DE AltName: Full=2-phospho-D-glycerate hydro-lyase; GN Name=ERR1; OrderedLocusNames=YOR393W; GN and GN Name=ERR2; OrderedLocusNames=YPL281C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (YOR393W). RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97313270; PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., RA Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., RA Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., RA Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., RA Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., RA Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., RA Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., RA Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., RA Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., RA Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., RA Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., RA Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., RA Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., RA Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., RA Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (YPL281C). RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313271; PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., RA Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., RA Zollner A., Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-437 (YOR393W). RC STRAIN=ATCC 90839 / S288c / YP1; RX MEDLINE=95304851; PubMed=7785338; DOI=10.1002/yea.320110410; RA Pryde F.E., Huckle T.C., Louis E.J.; RT "Sequence analysis of the right end of chromosome XV in Saccharomyces RT cerevisiae: an insight into the structural and functional significance RT of sub-telomeric repeat sequences."; RL Yeast 11:371-382(1995). CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + CC H(2)O. CC -!- COFACTOR: Magnesium (By similarity). CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. CC -!- INTERACTION: CC P53924:-; NbExp=1; IntAct=EBI-35679, EBI-28867; CC P47146:ABM1; NbExp=1; IntAct=EBI-35679, EBI-25611; CC Q06541:ARV1; NbExp=1; IntAct=EBI-35679, EBI-31952; CC P36075:CUE2; NbExp=1; IntAct=EBI-35679, EBI-26782; CC P36156:ECM4; NbExp=1; IntAct=EBI-35679, EBI-2042717; CC P53939:NIS1; NbExp=1; IntAct=EBI-35679, EBI-28760; CC Q06216:PIG1; NbExp=1; IntAct=EBI-35679, EBI-13413; CC P14906:SEC63; NbExp=1; IntAct=EBI-35679, EBI-16636; CC P47822:SRB7; NbExp=1; IntAct=EBI-35679, EBI-18046; CC P40318:SSM4; NbExp=1; IntAct=EBI-35679, EBI-18208; CC -!- SIMILARITY: Belongs to the enolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z75301; CAA99725.1; -; Genomic_DNA. DR EMBL; Z75302; CAA99728.1; -; Genomic_DNA. DR EMBL; Z73637; CAA98018.1; -; Genomic_DNA. DR EMBL; U23472; AAC48992.1; -; Genomic_DNA. DR PIR; S67305; S67305. DR RefSeq; NP_015038.1; -. DR RefSeq; NP_015042.1; -. DR HSSP; Q9NDH8; 1OEP. DR DIP; DIP:8882N; -. DR IntAct; Q12007; 59. DR Ensembl; YOR393W; Saccharomyces cerevisiae. DR Ensembl; YPL281C; Saccharomyces cerevisiae. DR GeneID; 854575; -. DR GeneID; 855848; -. DR CYGD; YOR393w; -. DR CYGD; YPL281c; -. DR SGD; S000005920; ERR1. DR SGD; S000006202; ERR2. DR HOGENOM; Q12007; -. DR BRENDA; 4.2.1.11; 250. DR NextBio; 977033; -. DR GermOnline; YOR393W; Saccharomyces cerevisiae. DR GermOnline; YPL281C; Saccharomyces cerevisiae. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW. DR InterPro; IPR000941; Enolase. DR PANTHER; PTHR11902; Enolase; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR ProDom; PD000902; Enolase; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycolysis; Lyase; Magnesium; Metal-binding. FT CHAIN 1 437 Enolase-related protein 1/2. FT /FTId=PRO_0000134064. FT REGION 373 376 Substrate binding (By similarity). FT ACT_SITE 212 212 Proton donor (By similarity). FT ACT_SITE 346 346 Proton acceptor (By similarity). FT METAL 247 247 Magnesium (By similarity). FT METAL 296 296 Magnesium (By similarity). FT METAL 321 321 Magnesium (By similarity). FT BINDING 160 160 Substrate (By similarity). FT BINDING 169 169 Substrate (By similarity). FT BINDING 296 296 Substrate (By similarity). FT BINDING 321 321 Substrate (By similarity). FT BINDING 397 397 Substrate (By similarity). FT CONFLICT 231 231 E -> K (in Ref. 3; AAC48992). SQ SEQUENCE 437 AA; 47328 MW; FAF09C00BE0E711C CRC64; MSITKVHART VYDSRGNPTV EVEITTENGL FRAIVPSGAS TGIHEAVELR DGNKSEWMGK GVTKAVSNVN SIIGPALIKS ELCVTNQKGI DELMISLDGT SNKSRLGANA ILGVSLCVAR AAAAQKGITL YKYIAELADA RQDPFVIPVP FFNVLNGGAH AGGSLAMQEF KIAPVGAQSF AEAMRMGSEV YHHLKILAKE QYGPSAGNVG DEGGVAPDID TAEDALDMIV EAINICGYEG RVKVGIDSAP SVFYKDGKYD LNFKEPNSDP SHWLSPAQLA EYYHSLLKKY PIISLEDPYA EDDWSSWSAF LKTVNVQIIA DDLTCTNKTR IARAIEEKCA NTLLLKLNQI GTLTESIEAA NQAFDAGWGV MISHRSGETE DPFIADLVVG LRCGQIKSGA LSRSERLAKY NELLRIEEEL GDDCIYAGHR FHDGNKL //