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Database: UniProt
Entry: I3VVW4_THESW
LinkDB: I3VVW4_THESW
Original site: I3VVW4_THESW 
ID   I3VVW4_THESW            Unreviewed;       195 AA.
AC   I3VVW4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE            EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN   OrderedLocusNames=Tsac_1653 {ECO:0000313|EMBL:AFK86659.1};
OS   Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK86659.1, ECO:0000313|Proteomes:UP000006178};
RN   [1] {ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA   Brown S.D., Land M.L., Herring C.D.;
RT   "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFK86659.1, ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX   PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA   Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA   Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT   "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT   Thermoanaerobacterium saccharolyticum during the Degradation of
RT   Hemicellulose.";
RL   Appl. Environ. Microbiol. 80:5001-5011(2014).
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; CP003184; AFK86659.1; -; Genomic_DNA.
DR   RefSeq; WP_014758525.1; NC_017992.1.
DR   AlphaFoldDB; I3VVW4; -.
DR   STRING; 1094508.Tsac_1653; -.
DR   KEGG; tsh:Tsac_1653; -.
DR   PATRIC; fig|1094508.3.peg.1674; -.
DR   eggNOG; COG1648; Bacteria.
DR   BioCyc; TSAC1094508:GLMA-1676-MONOMER; -.
DR   UniPathway; UPA00262; UER00222.
DR   Proteomes; UP000006178; 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; 1.10.8.610; SirC, precorrin-2 dehydrogenase, C-terminal helical domain-like; 1.
DR   InterPro; IPR028161; Met8-like.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR042518; SirC_C.
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; 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   Coiled coil {ECO:0000256|SAM:Coils}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244}.
FT   DOMAIN          120..145
FT                   /note="Siroheme synthase central"
FT                   /evidence="ECO:0000259|Pfam:PF14824"
FT   COILED          144..175
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   195 AA;  22191 MW;  E14B8D3B811B275F CRC64;
     MAYYPIMLNI LDKKCLVIGG GKVAYRKILP LLEFGATVTA LSSYFTDEIL ELPKNHKVNL
     IRRSYQKNDV DNYFLVVVAT NDRIINKEIS NECKKKNILV NVVDDKELST FIVPSVMKKG
     DLTISVSTNG KSPLLAKRIK EMLGNMFEDD VENLIAELSN LRDKLKTTSA TQEEKIKLYD
     DIINKYNILR GNDKK
//
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