ID MET8_YEAST STANDARD; PRT; 274 AA. AC P15807; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Siroheme biosynthesis protein MET8 [Includes: Precorrin-2 DE dehydrogenase (EC 1.3.1.76); Sirohydrochlorin ferrochelatase DE (EC 4.99.1.4)]. GN Name=MET8; OrderedLocusNames=YBR213W; ORFNames=YBR1461; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=X2180-1A; RX MEDLINE=90174997; PubMed=2408020; 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=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 H., 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 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 [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 11-274. 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: Sirohydrochlorin + Fe(2+) = siroheme + 2 H(+). CC -!- PATHWAY: Siroheme biosynthesis; second step. CC -!- PATHWAY: Siroheme biosynthesis; third step. CC -!- SIMILARITY: To S.pombe SpAC4D7.06c. 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; -. DR EMBL; Z36082; CAA85177.1; -. DR PIR; S20155; S20155. DR PDB; 1KYQ; X-ray; A/B/C=1-274. DR GermOnline; 138756; -. DR SGD; S000000417; MET8. DR GO; GO:0004325; F:ferrochelatase activity; IDA. DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IDA. DR GO; GO:0019354; P:siroheme biosynthesis; IMP. DR GO; GO:0000103; P:sulfate assimilation; IMP. DR InterPro; IPR006367; CysG_synth_N. DR PIRSF; PIRSF004999; Precr_oxd_chelt; 1. DR TIGRFAMs; TIGR01470; cysG_Nterm; 1. KW 3D-structure; Complete proteome; Lyase; Methionine biosynthesis; KW Multifunctional enzyme; NAD; Oxidoreductase; Porphyrin biosynthesis. FT ACT_SITE 141 141 Base proton acceptor. FT CONFLICT 15 15 K -> R (in Ref. 4). FT CONFLICT 33 33 I -> M (in Ref. 4). FT CONFLICT 61 61 E -> K (in Ref. 4). FT CONFLICT 102 102 D -> N (in Ref. 4). FT STRAND 5 9 FT TURN 12 13 FT STRAND 15 21 FT HELIX 23 32 FT HELIX 33 35 FT TURN 36 36 FT STRAND 38 46 FT TURN 48 49 FT HELIX 50 54 FT HELIX 56 58 FT STRAND 72 74 FT TURN 76 77 FT TURN 80 81 FT STRAND 87 89 FT HELIX 95 98 FT TURN 103 104 FT STRAND 107 112 FT HELIX 117 131 FT TURN 133 134 FT STRAND 136 139 FT TURN 140 141 FT HELIX 143 145 FT STRAND 146 146 FT STRAND 148 149 FT STRAND 152 156 FT TURN 157 159 FT STRAND 160 166 FT HELIX 171 188 FT HELIX 193 210 FT HELIX 214 216 FT HELIX 217 235 FT HELIX 236 238 FT STRAND 239 239 FT HELIX 241 252 FT TURN 253 256 FT HELIX 264 270 FT STRAND 272 272 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 //