SIRC_BACSU
ID SIRC_BACSU Reviewed; 162 AA.
AC O34813; Q796I3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Precorrin-2 dehydrogenase;
DE EC=1.3.1.76;
GN Name=sirC; Synonyms=ylnF; OrderedLocusNames=BSU15630;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Foulger D., Errington J.;
RT "Cloning and sequencing 8 Kbp of DNA from Bacillus subtilis downstream of
RT the pyr operon.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION IN SIROHEME SYNTHESIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=10217486; DOI=10.1099/13500872-145-3-529;
RA Johansson P., Hederstedt L.;
RT "Organization of genes for tetrapyrrole biosynthesis in Gram-positive
RT bacteria.";
RL Microbiology 145:529-538(1999).
RN [4]
RP INDUCTION.
RC STRAIN=168 / JH642;
RX PubMed=11004190; DOI=10.1128/jb.182.20.5885-5892.2000;
RA Mansilla M.C., Albanesi D., de Mendoza D.;
RT "Transcriptional control of the sulfur-regulated cysH operon, containing
RT genes involved in L-cysteine biosynthesis in Bacillus subtilis.";
RL J. Bacteriol. 182:5885-5892(2000).
CC -!- FUNCTION: Catalyzes the dehydrogenation of precorrin-2 to form
CC sirohydrochlorin which is used as a precursor in both siroheme
CC biosynthesis and in the anaerobic branch of adenosylcobalamin
CC biosynthesis. {ECO:0000305|PubMed:10217486}.
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 -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC sirohydrochlorin from precorrin-2: step 1/1.
CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
CC -!- INDUCTION: Up-regulated by sulfur starvation and repressed by cysteine.
CC Also induced by O-acetyl-L-serine (OAS), a direct precursor of
CC cysteine, maybe via inactivation of a putative transcriptional
CC repressor of the cysH operon whose activity is controlled by the
CC intracellular levels of OAS. {ECO:0000269|PubMed:11004190}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC minimal medium with nitrate as nitrogen source. Growth is restored only
CC after addition of both cysteine and ammonia to the medium.
CC {ECO:0000269|PubMed:10217486}.
CC -!- SIMILARITY: Belongs to the precorrin-2 dehydrogenase / sirohydrochlorin
CC ferrochelatase family. {ECO:0000305}.
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DR EMBL; AJ000974; CAA04415.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13437.1; -; Genomic_DNA.
DR PIR; F69877; F69877.
DR RefSeq; NP_389446.1; NC_000964.3.
DR RefSeq; WP_003232091.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34813; -.
DR SMR; O34813; -.
DR STRING; 224308.BSU15630; -.
DR PaxDb; O34813; -.
DR PRIDE; O34813; -.
DR EnsemblBacteria; CAB13437; CAB13437; BSU_15630.
DR GeneID; 938048; -.
DR KEGG; bsu:BSU15630; -.
DR PATRIC; fig|224308.179.peg.1703; -.
DR eggNOG; COG1648; Bacteria.
DR InParanoid; O34813; -.
DR OMA; VYMPKIV; -.
DR PhylomeDB; O34813; -.
DR BioCyc; BSUB:BSU15630-MON; -.
DR UniPathway; UPA00148; UER00222.
DR UniPathway; UPA00262; UER00222.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:InterPro.
DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019354; P:siroheme biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cobalamin biosynthesis; NAD; Oxidoreductase; Porphyrin biosynthesis;
KW Reference proteome.
FT CHAIN 1..162
FT /note="Precorrin-2 dehydrogenase"
FT /id="PRO_0000378490"
FT BINDING 20..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 41..42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 162 AA; 18004 MW; D8A54B4DEAF1E94E CRC64;
MLPLHISLEK KKVVIAGGGS IALRRLKTVI SEGADITLVS PDVEPEIKQM AEERRIKWEK
RTIEKEDYLN AFFIIAATDN AAVNKEIAQS ASPFQLVNCV SDAELGNVYM PKIVKRGHVT
VSVSTSGASP KHTKELAENV DKLIDGDFVA EVNRLYQMRR KK
