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Siroheme biosynthesis protein MET8 [Includes: Precorrin-2 dehydrogenase (EC 1.3.1.76); Sirohydrochlorin ferrochelatase (EC 4.99.1.4)]

 MET8_YEAST              Reviewed;         274 AA.
P15807; D6VQK9;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
12-SEP-2018, entry version 165.
RecName: Full=Siroheme biosynthesis protein MET8;
Includes:
RecName: Full=Precorrin-2 dehydrogenase;
EC=1.3.1.76;
Includes:
RecName: Full=Sirohydrochlorin ferrochelatase;
EC=4.99.1.4;
Name=MET8; OrderedLocusNames=YBR213W; ORFNames=YBR1461;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 26786 / X2180-1A;
PubMed=2408020; DOI=10.1093/nar/18.3.659;
Cherest H., Thomas D., Surdin-Kerjan Y.;
"Nucleotide sequence of the MET8 gene of Saccharomyces cerevisiae.";
Nucleic Acids Res. 18:659-659(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION.
PubMed=10051442; DOI=10.1042/bj3380701;
Raux E., McVeigh T., Peters S.E., Leustek T., Warren M.J.;
"The role of Saccharomyces cerevisiae Met1p and Met8p in sirohaem and
cobalamin biosynthesis.";
Biochem. J. 338:701-708(1999).
[5]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 11-274 IN COMPLEX WITH NAD,
SUBUNIT, AND MUTAGENESIS OF GLY-22; ASP-141 AND HIS-237.
PubMed=11980703; DOI=10.1093/emboj/21.9.2068;
Schubert H.L., Raux E., Brindley A.A., Leech H.K., Wilson K.S.,
Hill C.P., Warren M.J.;
"The structure of Saccharomyces cerevisiae Met8p, a bifunctional
dehydrogenase and ferrochelatase.";
EMBO J. 21:2068-2075(2002).
-!- FUNCTION: Catalyzes the conversion of precorrin-2 into siroheme.
This reaction consist of the NAD-dependent oxidation of precorrin-
2 into sirohydrochlorin and its subsequent ferrochelation into
siroheme. {ECO:0000269|PubMed:10051442}.
-!- CATALYTIC ACTIVITY: Precorrin-2 + NAD(+) = sirohydrochlorin +
NADH.
-!- CATALYTIC ACTIVITY: Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+).
-!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
biosynthesis; siroheme from sirohydrochlorin: step 1/1.
-!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11980703}.
-!- SIMILARITY: Belongs to the precorrin-2 dehydrogenase /
sirohydrochlorin ferrochelatase family. MET8 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X17271; CAA35173.1; -; Genomic_DNA.
EMBL; Z36082; CAA85177.1; -; Genomic_DNA.
EMBL; BK006936; DAA07329.1; -; Genomic_DNA.
PIR; S20155; S20155.
RefSeq; NP_009772.1; NM_001178561.1.
PDB; 1KYQ; X-ray; 2.20 A; A/B/C=1-274.
PDBsum; 1KYQ; -.
ProteinModelPortal; P15807; -.
SMR; P15807; -.
BioGrid; 32910; 109.
DIP; DIP-4944N; -.
IntAct; P15807; 2.
MINT; P15807; -.
STRING; 4932.YBR213W; -.
iPTMnet; P15807; -.
MaxQB; P15807; -.
PaxDb; P15807; -.
PRIDE; P15807; -.
EnsemblFungi; YBR213W; YBR213W; YBR213W.
GeneID; 852514; -.
KEGG; sce:YBR213W; -.
EuPathDB; FungiDB:YBR213W; -.
SGD; S000000417; MET8.
HOGENOM; HOG000181024; -.
InParanoid; P15807; -.
KO; K02304; -.
OMA; VSDTYKW; -.
OrthoDB; EOG092C3NWX; -.
BioCyc; MetaCyc:G3O-29150-MONOMER; -.
BioCyc; YEAST:G3O-29150-MONOMER; -.
BRENDA; 1.3.1.76; 984.
BRENDA; 4.99.1.4; 984.
UniPathway; UPA00262; UER00222.
UniPathway; UPA00262; UER00376.
EvolutionaryTrace; P15807; -.
PRO; PR:P15807; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0004325; F:ferrochelatase activity; IDA:SGD.
GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central.
GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IDA:SGD.
GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:UniProtKB-EC.
GO; GO:0019354; P:siroheme biosynthetic process; IMP:SGD.
GO; GO:0000103; P:sulfate assimilation; IMP:SGD.
InterPro; IPR028161; Met8.
InterPro; IPR028162; Met8_C.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR028281; Sirohaem_synthase_central.
PANTHER; PTHR35330; PTHR35330; 1.
Pfam; PF14823; Sirohm_synth_C; 1.
Pfam; PF14824; Sirohm_synth_M; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis; Complete proteome; Lyase;
Methionine biosynthesis; Multifunctional enzyme; NAD; Oxidoreductase;
Porphyrin biosynthesis; Reference proteome.
CHAIN 1 274 Siroheme biosynthesis protein MET8.
/FTId=PRO_0000096446.
NP_BIND 23 24 NAD. {ECO:0000269|PubMed:11980703}.
NP_BIND 43 45 NAD. {ECO:0000269|PubMed:11980703}.
ACT_SITE 141 141 Proton acceptor. {ECO:0000255}.
BINDING 93 93 NAD; via amide nitrogen.
{ECO:0000269|PubMed:11980703}.
MUTAGEN 22 22 G->D: Loss of dehydrogenase activity. No
effect on chelatase activity.
{ECO:0000269|PubMed:11980703}.
MUTAGEN 141 141 D->A: Loss of chelatase and dehydrogenase
activity. {ECO:0000269|PubMed:11980703}.
MUTAGEN 237 237 H->A: No effect on dehydrogenase or
chelatase activity.
{ECO:0000269|PubMed:11980703}.
CONFLICT 15 15 K -> R (in Ref. 5). {ECO:0000305}.
CONFLICT 33 33 I -> M (in Ref. 5). {ECO:0000305}.
CONFLICT 61 61 E -> K (in Ref. 5). {ECO:0000305}.
CONFLICT 102 102 D -> N (in Ref. 5). {ECO:0000305}.
STRAND 5 9 {ECO:0000244|PDB:1KYQ}.
STRAND 15 22 {ECO:0000244|PDB:1KYQ}.
HELIX 23 32 {ECO:0000244|PDB:1KYQ}.
HELIX 33 35 {ECO:0000244|PDB:1KYQ}.
STRAND 38 46 {ECO:0000244|PDB:1KYQ}.
HELIX 50 54 {ECO:0000244|PDB:1KYQ}.
HELIX 56 58 {ECO:0000244|PDB:1KYQ}.
TURN 68 70 {ECO:0000244|PDB:1KYQ}.
STRAND 72 74 {ECO:0000244|PDB:1KYQ}.
STRAND 86 89 {ECO:0000244|PDB:1KYQ}.
HELIX 95 98 {ECO:0000244|PDB:1KYQ}.
STRAND 107 112 {ECO:0000244|PDB:1KYQ}.
HELIX 117 131 {ECO:0000244|PDB:1KYQ}.
STRAND 135 139 {ECO:0000244|PDB:1KYQ}.
HELIX 143 145 {ECO:0000244|PDB:1KYQ}.
STRAND 146 149 {ECO:0000244|PDB:1KYQ}.
STRAND 152 156 {ECO:0000244|PDB:1KYQ}.
TURN 157 159 {ECO:0000244|PDB:1KYQ}.
STRAND 160 169 {ECO:0000244|PDB:1KYQ}.
HELIX 171 188 {ECO:0000244|PDB:1KYQ}.
HELIX 193 210 {ECO:0000244|PDB:1KYQ}.
HELIX 214 216 {ECO:0000244|PDB:1KYQ}.
HELIX 217 235 {ECO:0000244|PDB:1KYQ}.
HELIX 236 238 {ECO:0000244|PDB:1KYQ}.
HELIX 241 252 {ECO:0000244|PDB:1KYQ}.
TURN 253 256 {ECO:0000244|PDB:1KYQ}.
HELIX 264 270 {ECO:0000244|PDB:1KYQ}.
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


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