PC2DH_METBF
ID PC2DH_METBF Reviewed; 224 AA.
AC Q46CH4;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Precorrin-2 dehydrogenase;
DE Short=Mba_PC2_DH;
DE EC=1.3.1.76;
GN OrderedLocusNames=Mbar_A1461;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=21197080; DOI=10.1155/2010/175050;
RA Storbeck S., Rolfes S., Raux-Deery E., Warren M.J., Jahn D., Layer G.;
RT "A novel pathway for the biosynthesis of heme in Archaea: genome-based
RT bioinformatic predictions and experimental evidence.";
RL Archaea 2010:175050-175050(2010).
CC -!- FUNCTION: Involved in the archaeal biosynthesis of heme. Catalyzes the
CC oxiation of precorrin-2 into sirohydroclorin.
CC {ECO:0000269|PubMed:21197080}.
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 Evidence={ECO:0000269|PubMed:21197080};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin
CC ferrochelatase family. {ECO:0000305}.
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DR EMBL; CP000099; AAZ70418.1; -; Genomic_DNA.
DR RefSeq; WP_011306464.1; NC_007355.1.
DR AlphaFoldDB; Q46CH4; -.
DR SMR; Q46CH4; -.
DR STRING; 269797.Mbar_A1461; -.
DR EnsemblBacteria; AAZ70418; AAZ70418; Mbar_A1461.
DR GeneID; 3627742; -.
DR KEGG; mba:Mbar_A1461; -.
DR eggNOG; arCOG01044; Archaea.
DR HOGENOM; CLU_011276_8_1_2; -.
DR OMA; THVVVPY; -.
DR OrthoDB; 94240at2157; -.
DR UniPathway; UPA00262; UER00222.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:InterPro.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0019354; P:siroheme biosynthetic process; IDA:UniProtKB.
DR Gene3D; 1.10.8.610; -; 1.
DR InterPro; IPR028161; Met8.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042518; SirC_C.
DR InterPro; IPR006367; Sirohaem_synthase_N.
DR PANTHER; PTHR35330; PTHR35330; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01470; cysG_Nterm; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Porphyrin biosynthesis.
FT CHAIN 1..224
FT /note="Precorrin-2 dehydrogenase"
FT /id="PRO_0000428884"
FT BINDING 26..27
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 47..50
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 224 AA; 24736 MW; 7529FB0E22618AA7 CRC64;
MTKTNNFLPL MLDLSGRKIV IFGGGSVGER KAKLFSGCAD TLVASLEFSQ ALQELGTSGQ
VRLVQLDLLT ASDSELRGLI SGAFLVIPAT SNFELNQKIT AIARENDILI NQVDTLGSVV
IPSVIKRGDL VIGISTLGHS PAVSKYTRKQ IEGLVTPEYS DMIRLQDELR SYLKQHVAEQ
RERKEILWKV LESETVWNGF SESYEKAAER AYAIISSYLV NSNR
