ID A7GMW7_BACCN Unreviewed; 205 AA.
AC A7GMW7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN OrderedLocusNames=Bcer98_1150 {ECO:0000313|EMBL:ABS21475.1};
OS Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS21475.1, ECO:0000313|Proteomes:UP000002300};
RN [1] {ECO:0000313|EMBL:ABS21475.1, ECO:0000313|Proteomes:UP000002300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC {ECO:0000313|Proteomes:UP000002300};
RX PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "Extending the Bacillus cereus group genomics to putative food-borne
RT pathogens of different toxicity.";
RL Chem. Biol. Interact. 171:236-249(2008).
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; CP000764; ABS21475.1; -; Genomic_DNA.
DR RefSeq; WP_011984228.1; NC_009674.1.
DR AlphaFoldDB; A7GMW7; -.
DR STRING; 315749.Bcer98_1150; -.
DR GeneID; 56416735; -.
DR KEGG; bcy:Bcer98_1150; -.
DR eggNOG; COG1648; Bacteria.
DR HOGENOM; CLU_011276_8_1_9; -.
DR OrthoDB; 9773765at2; -.
DR UniPathway; UPA00262; UER00222.
DR Proteomes; UP000002300; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244}.
FT DOMAIN 116..141
FT /note="Siroheme synthase central"
FT /evidence="ECO:0000259|Pfam:PF14824"
SQ SEQUENCE 205 AA; 23304 MW; 1968AA2644964FCA CRC64;
MYPLTVRIEN KRVVVIGGGK VAGFKIIPLL NQGANIIVVS PKLDASLVKL VESKKIRWYQ
KEYENGDLEG AFLVVAATSD PFLNERIEKD AGTNQLVNVI TNPEKGNVHF PSTIHRGKLN
IAVSTGGASP KLAKKIRDEI AHKYGEIYET YLEFLYEVRR KVKELQLEKR EQNRMLQEVL
KPIYLQKETE RELFLQALEK KSQVG
//
