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Database: UniProt
Entry: O34632
LinkDB: O34632
Original site: O34632 
ID   SIRB_BACSU              Reviewed;         261 AA.
AC   O34632;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   29-SEP-2021, entry version 110.
DE   RecName: Full=Sirohydrochlorin ferrochelatase;
DE            EC=4.99.1.4;
GN   Name=sirB; Synonyms=ylnE; OrderedLocusNames=BSU15620;
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   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: Chelates iron to the siroheme precursor. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + siroheme = Fe(2+) + sirohydrochlorin;
CC         Xref=Rhea:RHEA:24360, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:58351, ChEBI:CHEBI:60052; EC=4.99.1.4;
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
CC       biosynthesis; siroheme from sirohydrochlorin: 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   -!- SIMILARITY: Belongs to the CbiX family. SirB subfamily. {ECO:0000305}.
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DR   EMBL; AJ000974; CAA04414.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13436.1; -; Genomic_DNA.
DR   PIR; E69877; E69877.
DR   RefSeq; NP_389445.1; NC_000964.3.
DR   RefSeq; WP_003232093.1; NZ_JNCM01000035.1.
DR   PDB; 5ZT7; X-ray; 2.94 A; A/B=1-261.
DR   PDB; 5ZT8; X-ray; 2.00 A; A/B=1-261.
DR   PDB; 5ZT9; X-ray; 2.80 A; A/B=1-261.
DR   PDB; 5ZTA; X-ray; 3.07 A; A/B=1-261.
DR   PDBsum; 5ZT7; -.
DR   PDBsum; 5ZT8; -.
DR   PDBsum; 5ZT9; -.
DR   PDBsum; 5ZTA; -.
DR   SMR; O34632; -.
DR   STRING; 224308.BSU15620; -.
DR   PaxDb; O34632; -.
DR   PRIDE; O34632; -.
DR   DNASU; 936218; -.
DR   EnsemblBacteria; CAB13436; CAB13436; BSU_15620.
DR   GeneID; 936218; -.
DR   KEGG; bsu:BSU15620; -.
DR   PATRIC; fig|224308.179.peg.1702; -.
DR   eggNOG; COG2138; Bacteria.
DR   InParanoid; O34632; -.
DR   OMA; IGITHPR; -.
DR   PhylomeDB; O34632; -.
DR   BioCyc; BSUB:BSU15620-MONOMER; -.
DR   UniPathway; UPA00262; UER00376.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002762; CbiX-like.
DR   Pfam; PF01903; CbiX; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Iron; Lyase; Metal-binding; Porphyrin biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..261
FT                   /note="Sirohydrochlorin ferrochelatase"
FT                   /id="PRO_0000150366"
FT   METAL           10
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   METAL           76
FT                   /note="Iron"
FT                   /evidence="ECO:0000250"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   HELIX           15..28
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   STRAND          35..48
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   HELIX           49..58
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   STRAND          62..69
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   HELIX           75..78
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   HELIX           80..89
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   HELIX           107..118
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   STRAND          128..133
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   HELIX           139..155
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   STRAND          159..172
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   HELIX           173..179
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   HELIX           199..214
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   STRAND          216..220
FT                   /evidence="ECO:0007829|PDB:5ZT8"
FT   HELIX           228..243
FT                   /evidence="ECO:0007829|PDB:5ZT8"
SQ   SEQUENCE   261 AA;  28835 MW;  DB46510BA39CFF1F CRC64;
     MKQAILYVGH GSRVKKAQQE AAAFLEGCKA HISVPVQEIS FLELQEPTIE TGFEACVKQG
     ATHIAVVPLL LLTAAHAKHD IPEEIVRVAS RYPSVRISYG KPIGIDEEVV KAVYHRMKDI
     GVPYENARVV LIGRGSSDPD VKRDVTGIAN LLQEMVPVKE VIPCFLTACG PNYKEVFSEL
     EKDDGITTFI VPYLLFTGML MNEIEREVQK LKAHNPNVYL SSYIGFHPHV KNAFLNRVRE
     TAANSEGQFD FDGGSYASAA H
//
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