Q81TU9 (HEMH2_BACAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ferrochelatase 2
EC=4.99.1.1

Alternative name(s):
Heme synthase 2
Protoheme ferro-lyase 2

Gene names

Name:	hemH2
Synonyms:	hemH-2
Ordered Locus Names:	BA_1158, GBAA_1158, BAS1075

Organism

Bacillus anthracis

Taxonomic identifier

1392 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the ferrous insertion into protoporphyrin IX. HAMAP MF_00323
Catalytic activity	Protoheme + 2 H+ = protoporphyrin + Fe2+. HAMAP MF_00323
Pathway	Porphyrin metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1. HAMAP MF_00323
Subcellular location	Cytoplasm By similarity HAMAP MF_00323.
Sequence similarities	Belongs to the ferrochelatase family.

Ontologies

Keywords
Biological process	Heme biosynthesis Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	heme biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ferrochelatase activity Inferred from electronic annotation. Source: EC metal 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 – 319	319	Ferrochelatase 2 HAMAP MF_00323		PRO_0000175103
Sites
	Metal binding	181	1	Iron By similarity
	Metal binding	262	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q81TU9 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 1162A729411CAAE5	FASTA	319	36,366
	10 20 30 40 50 60 MKKKKIGLLV MAYGTPDSLD EVEAYYTHIR HGRKPSEEAL QDLIGRYKAI GGISPLAKIT 70 80 90 100 110 120 KEQAHKLTDS MNNMFTEYEF NCYLGLKHTA PFIEDAVEEM KRDGIEQAIS IVLAPHYSTF 130 140 150 160 170 180 SIKAYNERAI RLSEEIGGPV IKPIDQWYDE PKFISYWADQ IKETFTKIED KEKAVVIFSA 190 200 210 220 230 240 HSLPEKIIAA GDPYVEQLQH TADLIAAAAN IQNYTIGWQS AGNTPDPWIG PDVQDLTRDL 250 260 270 280 290 300 FEEYRYESFI YCPVGFVAEH LEVLYDNDYE CKVVTDELNA AYFRPNMPNA QSTFIDCLAT 310 IVSRKMKEIV DKELILNNN

References

[1]	"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M. Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton.
[2]	"Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor.
[3]	"Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016879 Genomic DNA. Translation: AAP25126.1. AE017334 Genomic DNA. Translation: AAT30249.1. AE017225 Genomic DNA. Translation: AAT53398.1.
RefSeq	NP_843640.1. NC_003997.3. YP_017774.1. NC_007530.2. YP_027347.1. NC_005945.1.
3D structure databases
ProteinModelPortal	Q81TU9.
SMR	Q81TU9. Positions 3-310.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q81TU9. 2 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000010545; EBBACP00000010301; EBBACG00000010537. EBBACT00000016912; EBBACP00000016533; EBBACG00000016903. EBBACT00000022666; EBBACP00000022151; EBBACG00000022657.
GeneID	1084775. 2816522. 2852557.
GenomeReviews	Gene locus BA_1158 in contig AE016879_GR. Gene locus BAS1075 in contig AE017225_GR. Gene locus GBAA_1158 in contig AE017334_GR.
KEGG	ban:BA_1158. bar:GBAA_1158. bat:BAS1075.
TIGR	BA_1158. GBAA_1158.
Phylogenomic databases
GeneTree	EBGT00050000002085.
HOGENOM	HBG697135.
OMA	LEPDIVD.
ProtClustDB	PRK12435.
Enzyme and pathway databases
BioCyc	BANT260799:BAS1075-MONOMER. BANT261594:GBAA1158-MONOMER.
Family and domain databases
HAMAP	MF_00323. Ferrochelatase. [Tree]
InterPro	IPR001015. Ferrochelatase. IPR019772. Ferrochelatase_AS. [Graphical view]
KO	K01772.
PANTHER	PTHR11108. Ferrochelatase. 1 hit.
Pfam	PF00762. Ferrochelatase. 1 hit. [Graphical view]
TIGRFAMs	TIGR00109. HemH. 1 hit.
PROSITE	PS00534. FERROCHELATASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HEMH2_BACAN

Accession

Primary (citable) accession number: Q81TU9
Secondary accession number(s): Q6I233, Q6KVW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	June 1, 2003
Last modified:	November 16, 2011
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program