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Database: UniProt
Entry: Q57605
LinkDB: Q57605
Original site: Q57605 
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   16-JAN-2019, entry version 100.
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 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales; 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.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., 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
CC       the 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;
CC         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 /
CC       sirohydrochlorin ferrochelatase family. {ECO:0000305}.
DR   EMBL; L77117; AAB98123.1; -; Genomic_DNA.
DR   PIR; E64317; E64317.
DR   RefSeq; WP_010869635.1; NC_000909.1.
DR   ProteinModelPortal; 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   eggNOG; COG1648; LUCA.
DR   InParanoid; Q57605; -.
DR   KO; K02304; -.
DR   OMA; RKNVEEY; -.
DR   OrthoDB; 94240at2157; -.
DR   PhylomeDB; Q57605; -.
DR   BioCyc; MJAN243232:G1GKE-150-MONOMER; -.
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   Complete proteome; NAD; Oxidoreductase; Porphyrin biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    206       Putative precorrin-2 dehydrogenase.
FT                                /FTId=PRO_0000106716.
FT   NP_BIND      20     21       NAD. {ECO:0000250}.
FT   NP_BIND      41     46       NAD. {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
//
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