HEMZ_BACSU
ID HEMZ_BACSU Reviewed; 501 AA.
AC Q796V8; O07537; O07538;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Oxygen-independent coproporphyrinogen-III oxidase-like protein HemZ;
DE EC=1.3.99.-;
GN Name=hemZ; Synonyms=yhaV, yhaW; OrderedLocusNames=BSU09840;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
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 SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RX PubMed=10498703; DOI=10.1128/jb.181.19.5922-5929.1999;
RA Homuth G., Rompf A., Schumann W., Jahn D.;
RT "Transcriptional control of Bacillus subtilis hemN and hemZ.";
RL J. Bacteriol. 181:5922-5929(1999).
RN [5]
RP COFACTOR, AND CAUTION.
RC STRAIN=168;
RA Hauert J.;
RL Thesis (1977), University of Geneva, Switzerland.
CC -!- FUNCTION: Involved in the biosynthesis of porphyrin-containing
CC compound. {ECO:0000269|PubMed:10498703}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|Ref.5, ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000269|Ref.5, ECO:0000305};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis.
CC -!- INDUCTION: Induced under anaerobic conditions and by hydrogen peroxide
CC stress. It is also dependent on induction by ResDE, Fnr and ArfM.
CC {ECO:0000269|PubMed:10498703}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate
CC coproporphyrin-III only under anaerobic conditions, however no obvious
CC respiratory growth phenotype is observed under anaerobic conditions.
CC The hemN hemZ double mutant do not abolish aerobic and anaerobic
CC respiratory growth, however a reduction of growth is observed.
CC {ECO:0000269|PubMed:10498703}.
CC -!- MISCELLANEOUS: HemZ is able to complement a S.typhimurium hemF hemN
CC double mutant under aerobic and anaerobic conditions, however under
CC anaerobic growth conditions, the double mutant complemented with hemZ
CC grows significantly faster. {ECO:0000305|PubMed:10498703}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. HemZ subfamily. {ECO:0000305}.
CC -!- CAUTION: Although the enzyme shows to be able to complement hemF hemN
CC double mutant and to accumulate coproporphyrinogen-III when the gene is
CC disrupted, no oxygen-independent coproporphyrinogen-III oxidase
CC activity has been shown. The exact role of this protein is still
CC unknown. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA74441.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA74454.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Y14080; CAA74454.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Y14080; CAA74441.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB12823.2; -; Genomic_DNA.
DR PIR; A69820; A69820.
DR PIR; H69819; H69819.
DR RefSeq; NP_388865.1; NC_000964.3.
DR RefSeq; WP_003245132.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q796V8; -.
DR SMR; Q796V8; -.
DR STRING; 224308.BSU09840; -.
DR PaxDb; Q796V8; -.
DR PRIDE; Q796V8; -.
DR DNASU; 937935; -.
DR EnsemblBacteria; CAB12823; CAB12823; BSU_09840.
DR GeneID; 937935; -.
DR KEGG; bsu:BSU09840; -.
DR PATRIC; fig|224308.179.peg.1056; -.
DR eggNOG; COG0635; Bacteria.
DR InParanoid; Q796V8; -.
DR OMA; GQESIYN; -.
DR PhylomeDB; Q796V8; -.
DR BioCyc; BSUB:BSU09840-MON; -.
DR UniPathway; UPA00251; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR023995; HemZ.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR PANTHER; PTHR13932; PTHR13932; 1.
DR PANTHER; PTHR13932:SF1; PTHR13932:SF1; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00310; oxygen-independent_coproporphy; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR03994; rSAM_HemZ; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Porphyrin biosynthesis; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..501
FT /note="Oxygen-independent coproporphyrinogen-III oxidase-
FT like protein HemZ"
FT /id="PRO_0000109955"
FT DOMAIN 163..405
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 234..235
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 501 AA; 57527 MW; 8E4C2373D1D9190D CRC64;
MQIKIEGIHD DRLHRPLQNI ANLFYEECEL AYGGEEPADF VISLALSQTD EHVTVSGEVK
GTGIKEQHTK FFSPDMTEKE AFKQVKNTIS YVYLNLLQAH TGITQKWGIL TGIRPTKLLH
KKLQSGMSKE QAHAELKKDY LIHDEKIMLM QEIVDRQLAA VPDLYRVKDE VSIYIGIPFC
PTKCAYCTFP AYAIQGQAGR VGSFLWGLHY EMQKIGEWLK EHDVKVTTIY FGGGTPTSIT
AEEMDLLYEE MVRSFPDVKN IREITVEAGR PDTITEEKLA VLNKYDIDRI SINPQSYENE
TLKAIGRHHT VEETIEKYHL SRQHGMNNIN MDLIIGLPGE GVKEFRHSLS ETEKLMPESL
TVHTLSFKRA SEMTRNKHKY KVAGREEVSQ MMEDAVAWTK EHGYVPYYLY RQKNILGNLE
NVGYSLPGQE SIYNIMIMEE VQTIIGIGCG AASKFIDRDT GKITHFANPK DPKSYNERFE
HYTDEKIKYL EQIFEKTTKQ H
