ID MET8_YEAST Reviewed; 274 AA. AC P15807; D6VQK9; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 16-NOV-2011, entry version 109. DE RecName: Full=Siroheme biosynthesis protein MET8; DE Includes: DE RecName: Full=Precorrin-2 dehydrogenase; DE EC=1.3.1.76; DE Includes: DE RecName: Full=Sirohydrochlorin ferrochelatase; DE EC=4.99.1.4; GN Name=MET8; OrderedLocusNames=YBR213W; ORFNames=YBR1461; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 26786 / X2180-1A; RX MEDLINE=90174997; PubMed=2408020; DOI=10.1093/nar/18.3.659; RA Cherest H., Thomas D., Surdin-Kerjan Y.; RT "Nucleotide sequence of the MET8 gene of Saccharomyces cerevisiae."; RL Nucleic Acids Res. 18:659-659(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=95112788; PubMed=7813418; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., RA Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., RA Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., RA Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., RA Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., RA Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., RA Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., RA Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., RA Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., RA Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., RA Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., RA van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., RA Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., RA Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RG Saccharomyces Genome Database; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION. RX MEDLINE=99162236; PubMed=10051442; DOI=10.1042/0264-6021:3380701; RA Raux E., McVeigh T., Peters S.E., Leustek T., Warren M.J.; RT "The role of Saccharomyces cerevisiae Met1p and Met8p in sirohaem and RT cobalamin biosynthesis."; RL Biochem. J. 338:701-708(1999). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 11-274 IN COMPLEX WITH NAD, RP SUBUNIT, AND MUTAGENESIS OF GLY-22; ASP-141 AND HIS-237. RX MEDLINE=21977287; PubMed=11980703; DOI=10.1093/emboj/21.9.2068; RA Schubert H.L., Raux E., Brindley A.A., Leech H.K., Wilson K.S., RA Hill C.P., Warren M.J.; RT "The structure of Saccharomyces cerevisiae Met8p, a bifunctional RT dehydrogenase and ferrochelatase."; RL EMBO J. 21:2068-2075(2002). CC -!- FUNCTION: Catalyzes the conversion of precorrin-2 into siroheme. CC This reaction consist of the NAD-dependent oxidation of precorrin- CC 2 into sirohydrochlorin and its subsequent ferrochelation into CC siroheme. CC -!- CATALYTIC ACTIVITY: Precorrin-2 + NAD(+) = sirohydrochlorin + CC NADH. CC -!- CATALYTIC ACTIVITY: Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+). CC -!- PATHWAY: Porphyrin metabolism; siroheme biosynthesis; siroheme CC from sirohydrochlorin: step 1/1. CC -!- PATHWAY: Porphyrin metabolism; siroheme biosynthesis; CC sirohydrochlorin from precorrin-2: step 1/1. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the MET8 family. 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; X17271; CAA35173.1; -; Genomic_DNA. DR EMBL; Z36082; CAA85177.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07329.1; -; Genomic_DNA. DR PIR; S20155; S20155. DR RefSeq; NP_009772.1; NM_001178561.1. DR PDB; 1KYQ; X-ray; 2.20 A; A/B/C=1-274. DR PDBsum; 1KYQ; -. DR ProteinModelPortal; P15807; -. DR SMR; P15807; 1-273. DR DIP; DIP-4944N; -. DR IntAct; P15807; 1. DR MINT; MINT-553462; -. DR STRING; P15807; -. DR EnsemblFungi; YBR213W; YBR213W; YBR213W. DR GeneID; 852514; -. DR KEGG; sce:YBR213W; -. DR NMPDR; fig|4932.3.peg.483; -. DR CYGD; YBR213w; -. DR SGD; S000000417; MET8. DR GeneTree; EFGT00050000004881; -. DR HOGENOM; HBG204207; -. DR OMA; DGPLQIM; -. DR OrthoDB; EOG4578H4; -. DR PhylomeDB; P15807; -. DR BRENDA; 4.99.1.4; 984. DR NextBio; 971538; -. DR ArrayExpress; P15807; -. DR Genevestigator; P15807; -. DR GermOnline; YBR213W; Saccharomyces cerevisiae. DR GO; GO:0005488; F:binding; IEA:InterPro. DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IDA:SGD. DR GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:EC. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0019354; P:siroheme biosynthetic process; IMP:SGD. DR GO; GO:0000103; P:sulfate assimilation; IMP:SGD. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR023283; Siroheme_synth_dom_3. DR Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1. DR Gene3D; G3DSA:1.10.3280.10; Siroheme_synth_dom_3; 1. DR KO; K02304; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Lyase; KW Methionine biosynthesis; Multifunctional enzyme; NAD; Oxidoreductase; KW Porphyrin biosynthesis; Reference proteome. FT CHAIN 1 274 Siroheme biosynthesis protein MET8. FT /FTId=PRO_0000096446. FT NP_BIND 23 24 NAD. FT NP_BIND 43 45 NAD. FT ACT_SITE 141 141 Proton acceptor (Potential). FT BINDING 93 93 NAD; via amide nitrogen. FT MUTAGEN 22 22 G->D: Loss of dehydrogenase activity. No FT effect on chelatase activity. FT MUTAGEN 141 141 D->A: Loss of chelatase and dehydrogenase FT activity. FT MUTAGEN 237 237 H->A: No effect on dehydrogenase or FT chelatase activity. FT CONFLICT 15 15 K -> R (in Ref. 5). FT CONFLICT 33 33 I -> M (in Ref. 5). FT CONFLICT 61 61 E -> K (in Ref. 5). FT CONFLICT 102 102 D -> N (in Ref. 5). FT STRAND 5 9 FT STRAND 15 22 FT HELIX 23 32 FT HELIX 33 35 FT STRAND 38 46 FT HELIX 50 54 FT HELIX 56 58 FT STRAND 72 74 FT STRAND 86 89 FT HELIX 95 98 FT STRAND 107 112 FT HELIX 117 131 FT STRAND 135 139 FT HELIX 143 145 FT STRAND 146 149 FT STRAND 152 156 FT TURN 157 159 FT STRAND 160 169 FT HELIX 171 188 FT HELIX 193 210 FT HELIX 214 216 FT HELIX 217 235 FT HELIX 236 238 FT HELIX 241 252 FT TURN 253 256 FT HELIX 264 270 SQ SEQUENCE 274 AA; 31918 MW; 0EE9A6DE8A43673E CRC64; MVKSLQLAHQ LKDKKILLIG GGEVGLTRLY KLIPTGCKLT LVSPDLHKSI IPKFGKFIQN EDQPDYREDA KRFINPNWDP TKNEIYEYIR SDFKDEYLDL EDENDAWYII MTCIPDHPES ARIYHLCKER FGKQQLVNVA DKPDLCDFYF GANLEIGDRL QILISTNGLS PRFGALVRDE IRNLFTQMGD LALEDAVVKL GELRRGIRLL APDDKDVKYR MDWARRCTDL FGIQHCHNID VKRLLDLFKV MFQEQNCSLQ FPPRERLLSE YCSS //