ID MET8_SCHPO Reviewed; 264 AA.
AC O14172;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 128.
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; ORFNames=SPAC4D7.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the conversion of precorrin-2 into siroheme. This
CC reaction consist of the NAD-dependent oxidation of precorrin-2 into
CC sirohydrochlorin and its subsequent ferrochelation into siroheme (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin;
CC Xref=Rhea:RHEA:15613, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58351, ChEBI:CHEBI:58827; EC=1.3.1.76;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + siroheme = Fe(2+) + sirohydrochlorin;
CC Xref=Rhea:RHEA:24360, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:58351, ChEBI:CHEBI:60052; EC=4.99.1.4;
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; siroheme from sirohydrochlorin: step 1/1.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin
CC ferrochelatase family. MET8 subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB11278.1; -; Genomic_DNA.
DR PIR; T38797; T38797.
DR RefSeq; NP_594959.1; NM_001020390.2.
DR AlphaFoldDB; O14172; -.
DR SMR; O14172; -.
DR BioGRID; 280038; 29.
DR STRING; 284812.O14172; -.
DR iPTMnet; O14172; -.
DR MaxQB; O14172; -.
DR PaxDb; 4896-SPAC4D7-06c-1; -.
DR EnsemblFungi; SPAC4D7.06c.1; SPAC4D7.06c.1:pep; SPAC4D7.06c.
DR GeneID; 2543624; -.
DR KEGG; spo:SPAC4D7.06c; -.
DR PomBase; SPAC4D7.06c; met8.
DR VEuPathDB; FungiDB:SPAC4D7.06c; -.
DR eggNOG; ENOG502RYIW; Eukaryota.
DR HOGENOM; CLU_011276_8_5_1; -.
DR InParanoid; O14172; -.
DR OMA; STQIWKL; -.
DR PhylomeDB; O14172; -.
DR UniPathway; UPA00262; UER00222.
DR UniPathway; UPA00262; UER00376.
DR PRO; PR:O14172; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:UniProtKB-EC.
DR GO; GO:0019354; P:siroheme biosynthetic process; IBA:GO_Central.
DR GO; GO:0000103; P:sulfate assimilation; ISO:PomBase.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR028161; Met8-like.
DR InterPro; IPR028162; Met8_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028281; Sirohaem_synthase_central.
DR InterPro; IPR006367; Sirohaem_synthase_N.
DR NCBIfam; TIGR01470; cysG_Nterm; 1.
DR PANTHER; PTHR35330; SIROHEME BIOSYNTHESIS PROTEIN MET8; 1.
DR PANTHER; PTHR35330:SF1; SIROHEME BIOSYNTHESIS PROTEIN MET8; 1.
DR Pfam; PF13241; NAD_binding_7; 1.
DR Pfam; PF14823; Sirohm_synth_C; 1.
DR Pfam; PF14824; Sirohm_synth_M; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Multifunctional enzyme; NAD; Nucleus; Oxidoreductase;
KW Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..264
FT /note="Siroheme biosynthesis protein met8"
FT /id="PRO_0000346781"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 32..33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 53..56
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 264 AA; 29444 MW; 48AEF667DF3380F1 CRC64;
MASKYQSVQP GGSLIIAWRA QGKKVLIVGG GVVAAGRILH VLNADAHVIV VSPKAGLCKE
VAWRIQEKQV EWRDRGFLVE DLSDDVNMVL TAIDDPSLSS EIYKLCKSKK IPVNAADIPP
ECDFYFGSEI RNGPLQIMVS TNGKGPKLAS LIRKKIESSI NPATGMALEK TGLLRQKLRD
IVPEPENSRK RMRWMIEICE LWSLEELAML DENLINRLLG YFPKKTPSYR EITTPAYSKI
DNYIWFGAII ISGAVLLKHV SKAR
//
