SIRB_BACSU
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 03-AUG-2022, entry version 113.
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 AlphaFoldDB; O34632; -.
DR SMR; O34632; -.
DR STRING; 224308.BSU15620; -.
DR PaxDb; 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; WCAVRPA; -.
DR PhylomeDB; O34632; -.
DR BioCyc; BSUB:BSU15620-MON; -.
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 BINDING 10
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
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
