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Database: UniProt
Entry: D6E8X8_9ACTN
LinkDB: D6E8X8_9ACTN
Original site: D6E8X8_9ACTN 
ID   D6E8X8_9ACTN            Unreviewed;       217 AA.
AC   D6E8X8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE            EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN   ORFNames=GPA_16730 {ECO:0000313|EMBL:CBL04175.1};
OS   Gordonibacter pamelaeae 7-10-1-b.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Gordonibacter.
OX   NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL04175.1, ECO:0000313|Proteomes:UP000008805};
RN   [1] {ECO:0000313|EMBL:CBL04175.1, ECO:0000313|Proteomes:UP000008805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT   "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL04175.1, ECO:0000313|Proteomes:UP000008805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001156};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005010}.
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DR   EMBL; FP929047; CBL04175.1; -; Genomic_DNA.
DR   RefSeq; WP_015539524.1; NC_021021.1.
DR   AlphaFoldDB; D6E8X8; -.
DR   GeneID; 78360150; -.
DR   KEGG; gpa:GPA_16730; -.
DR   PATRIC; fig|657308.3.peg.1242; -.
DR   HOGENOM; CLU_011276_8_1_11; -.
DR   BioCyc; GPAM657308:GPA_RS07815-MONOMER; -.
DR   UniPathway; UPA00262; UER00222.
DR   Proteomes; UP000008805; Chromosome.
DR   GO; GO:0004325; F:ferrochelatase activity; IEA:InterPro.
DR   GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.8.210; Sirohaem synthase, dimerisation domain; 1.
DR   InterPro; IPR028161; Met8-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR037115; Sirohaem_synt_dimer_dom_sf.
DR   InterPro; IPR028281; Sirohaem_synthase_central.
DR   InterPro; IPR019478; Sirohaem_synthase_dimer_dom.
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; PF10414; CysG_dimeriser; 1.
DR   Pfam; PF13241; NAD_binding_7; 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   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:CBL04175.1}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:CBL04175.1};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008805}.
FT   DOMAIN          119..145
FT                   /note="Siroheme synthase central"
FT                   /evidence="ECO:0000259|Pfam:PF14824"
FT   DOMAIN          156..207
FT                   /note="Sirohaem synthase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF10414"
SQ   SEQUENCE   217 AA;  23474 MW;  CE958C169BADDE86 CRC64;
     MPTYPVSLVL QDRAALVVGG GAVATRKVEG LLPAGAHVTV VAPEVTEALR ALADAGRCAW
     RAKAYDAADL SGADIVFVAT DDEDVNARAY RDASGAHLMV NVADRPELCT FFLPSVLRRG
     KLSIAVSTEG ASPLTARRLR RELEERIPAG FETYLDLLAA WRPRAIAALP DEPARLRFWQ
     QATDGRVQRL VQAADEEAAE RLLEELLEAE RTACATL
//
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