Reviewed, UniProtKB/Swiss-Prot P54304 (HEMN_BACSU)

Names and origin

Protein names

Recommended name:
    Oxygen-independent coproporphyrinogen-III oxidase 1
      Short name=Coproporphyrinogenase
      Short name=Coprogen oxidase
    EC=1.3.99.22

Gene names

Name:	hemN
Synonyms:	yqeR
Ordered Locus Names:	BSU25500

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	379 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX By similarity.
Catalytic activity	Coproporphyrinogen-III + 2 S-adenosyl-L-methionine = protoporphyrinogen-IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine.
Cofactor	Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.
Pathway	Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route): step 1/1.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Induction	Induced, in anaerobic conditions, by resDE, fnr and arfM. Ref.6
Sequence similarities	Belongs to the anaerobic coproporphyrinogen-III oxidase family.

Ontologies

Keywords
Biological process	Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW porphyrin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW coproporphyrinogen dehydrogenase activity Inferred from electronic annotation. Source: EC coproporphyrinogen oxidase activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 379	379	Oxygen-independent coproporphyrinogen-III oxidase 1		PRO_0000109939
Regions
	Region	61 – 62	2	S-adenosyl-L-methionine 2 binding By similarity
Sites
	Metal binding	11	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	15	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	18	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Binding site	5	1	S-adenosyl-L-methionine 1 By similarity
	Binding site	17	1	S-adenosyl-L-methionine 2; via carbonyl oxygen By similarity
	Binding site	60	1	S-adenosyl-L-methionine 1; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	94	1	S-adenosyl-L-methionine 1 By similarity
	Binding site	121	1	S-adenosyl-L-methionine 2 By similarity
	Binding site	133	1	S-adenosyl-L-methionine 2 By similarity
	Binding site	158	1	S-adenosyl-L-methionine 2 By similarity
Experimental info
	Sequence conflict	94	1	E → D in BAA12461. Ref.2
	Sequence conflict	175	1	I → S in CAB61616. Ref.1
	Sequence conflict	365 – 379	15	KLLGN…FLGEL → NY in CAB61616. Ref.1
	Sequence conflict	365 – 379	15	KLLGN…FLGEL → NY in BAA12461. Ref.2
	Sequence conflict	365 – 379	15	KLLGN…FLGEL → NY in M84964. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P54304-1 [UniParc]. Last modified July 7, 2009. Version 3. Checksum: ECEC9FC2D638D3FF	FASTA	379	42,888
	10 20 30 40 50 60 MKSAYIHIPF CEHICHYCDF NKYFIQSQPV DEYLNALEQE MINTIAKTGQ PDLKTIFIGG 70 80 90 100 110 120 GTPTSLSEEQ LKKLMDMINR VLKPSSDLSE FAVEANPDDL SAEKLKILKE AGVNRLSFGV 130 140 150 160 170 180 QTFEDDLLEK IGRVHKQKDV FTSFERAREI GFENISLDLM FGLPGQTLKH LEHSINTALS 190 200 210 220 230 240 LDAEHYSVYS LIVEPKTVFY NLMQKGRLHL PPQEQEAEMY EIVMSKMEAH GIHQYEISNF 250 260 270 280 290 300 AKAGMESKHN LTYWSNEQYF GFGAGAHGYI GGTRTVNVGP VKHYIDLIAE KGFPYRDTHE 310 320 330 340 350 360 VTTEEQIEEE MFLGLRKTAG VSKKRFAEKY GRSLDGLFPS VLKDLAEKGL IHNSESAVYL 370 THQGKLLGNE VFGAFLGEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genes of lepA and hemN form a bicistronic operon in Bacillus subtilis." Homuth G., Heinemann M., Zuber U., Schumann W. Microbiology 142:1641-1649(1996) [PubMed: 8757728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes." Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y. Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 94 AND 365-379.
[5]	"Cloning, sequencing, and molecular analysis of the dnaK locus from Bacillus subtilis." Wetzstein M., Voelker U., Dedio J., Loebau S., Zuber U., Schiesswohl M., Herget C., Hecker M., Schumann W. J. Bacteriol. 174:3300-3310(1992) [PubMed: 1339421] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-366. Strain: 168 / MB11.
[6]	"Transcriptional control of Bacillus subtilis hemN and hemZ." Homuth G., Rompf A., Schumann W., Jahn D. J. Bacteriol. 181:5922-5929(1999) [PubMed: 10498703] [Abstract] Cited for: REGULATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X91655 Genomic DNA. Translation: CAB61616.1. D84432 Genomic DNA. Translation: BAA12461.1. AL009126 Genomic DNA. Translation: CAB14492.2. M84964 Genomic DNA. No translation available.
PIR	B69640.
RefSeq	NP_390428.2.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	937845.
GenomeReviews	Gene locus BSU25500 in contig AL009126_GR.
KEGG	bsu:BSU25500.
NMPDR	fig|224308.1.peg.2553.
Organism-specific databases
SubtiList	BG11395. hemN. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	HBG529648.
PhylomeDB	P54304.
Enzyme and pathway databases
BRENDA	1.3.99.22. 150.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR010723. HemN_C. IPR007197. Radical_SAM. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF06969. HemN_C. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
SMART	SM00729. Elp3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEMN_BACSU

Accession

Primary (citable) accession number: P54304

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 7, 2009
Last modified:	January 19, 2010
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)