hmoA

hmoA
168

heme monooxygenase

Locus
BSU_07150
Molecular weight
14.57 kDa
Isoelectric point
9.13
Protein length
125 aaSequenceBlast
Gene length
378 bpSequenceBlast
Function
degradation of heme
Product
heme monooxygenase
Essential
no
Synonyms
hmoA, yetG
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG2329 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
785,113  785,490
The protein
Catalyzed reaction/ biological activity
binds hemin in vitro with ~1:1 stoichiometry and degrades hemin in the presence of an electron donor PubMed
heme b + 3 O2 + 3 reduced [NADPH—hemoprotein reductase] --> biliverdin IXα + CO + Fe2+  + H+ + 3 H2O + 3 oxidized [NADPH—hemoprotein reductase] (according to UniProt)
Protein family
antibiotic biosynthesis monooxygenase family (with HmoB, according to UniProt)
Domains
ABM domain (aa 2-95) (according to UniProt)
Structure
1TZ0 (PDB) (from B. cereus, 57% identity)
O31534 (AlphaFold)
Localization
cytoplasm (according to Swiss-Prot)
Expression and Regulation
Operons
Genes
hmoA
Description
(based on genomic context) null
Regulation
induced by iron limitation (Fur) PubMed
Regulatory mechanism
Fur: repression, PubMed, in fur regulon
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hmoA

2025-03-29 07:55:04

ghost

68

0c7b16a020c2e8024e4ff7fa52d23836a7c6f3b8

E651851DF1274BBDC6F7E91633D91E05982D6F42

Biological materials
Mutant
MGNA-B458 (yetG::erm), available at the NBRP B. subtilis, Japan
BKE07150 (hmoA::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATTTGTCTCACTCCAATCA,  downstream forward: _UP4_TAAAAAGCTTGCGCCTTGCT
BKK07150 (hmoA::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATTTGTCTCACTCCAATCA,  downstream forward: _UP4_TAAAAAGCTTGCGCCTTGCT
References
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Time of last update: 2025-04-05 08:53:17

Author of last update: Jstuelk