PC2DH_METJA
ID PC2DH_METJA Reviewed; 206 AA.
AC Q57605;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative precorrin-2 dehydrogenase;
DE EC=1.3.1.76;
GN OrderedLocusNames=MJ0140;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Involved in the archaeal biosynthesis of heme. Catalyzes the
CC oxiation of precorrin-2 into sirohydroclorin (By similarity).
CC {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 -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin
CC ferrochelatase family. {ECO:0000305}.
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DR EMBL; L77117; AAB98123.1; -; Genomic_DNA.
DR PIR; E64317; E64317.
DR RefSeq; WP_010869635.1; NC_000909.1.
DR AlphaFoldDB; Q57605; -.
DR SMR; Q57605; -.
DR STRING; 243232.MJ_0140; -.
DR EnsemblBacteria; AAB98123; AAB98123; MJ_0140.
DR GeneID; 1450984; -.
DR KEGG; mja:MJ_0140; -.
DR eggNOG; arCOG01044; Archaea.
DR HOGENOM; CLU_011276_8_2_2; -.
DR InParanoid; Q57605; -.
DR OMA; THVVVPY; -.
DR OrthoDB; 94240at2157; -.
DR PhylomeDB; Q57605; -.
DR UniPathway; UPA00262; UER00222.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:InterPro.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0019354; P:siroheme biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR028161; Met8.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006367; Sirohaem_synthase_N.
DR PANTHER; PTHR35330; PTHR35330; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01470; cysG_Nterm; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Porphyrin biosynthesis; Reference proteome.
FT CHAIN 1..206
FT /note="Putative precorrin-2 dehydrogenase"
FT /id="PRO_0000106716"
FT BINDING 20..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 41..46
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 206 AA; 23989 MW; 50C36E48EE4FBC44 CRC64;
MLPILLSFEG KKVAVFGCGS VGKRRAKKIL KSGGIVDIYS KEFDEEIKKL KESNKNLNLI
EIDINQLSDE ELKNIIMKYD FIVTAINDEI NKRIVKLAKE LNKFVNSSTK TEGVNFIIPA
YTEVDEVIFS IYTKGKSPLI AKHIRIFVEN YLKSTDINMI AYIREFLKET IPKQKDREKI
LKKIFENEKF REELKKLIEK WENGNH
