Entry
Name
heme oxygenase (mycobilin-producing);
mhuD (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous
BRITE hierarchy
Sysname
protoheme,donor:oxygen oxidoreductase (mycobilin-producing)
Reaction(IUBMB)
(1) protoheme + 3 reduced acceptor + 3 O2 = mycobilin a + Fe2+ + 3 acceptor + 3 H2O [RN:
R11741 ];
(2) protoheme + 3 reduced acceptor + 3 O2 = mycobilin b + Fe2+ + 3 acceptor + 3 H2O [RN:
R11742 ]
Reaction(KEGG)
Substrate
Product
Comment
The enzyme, characterized from the bacterium Mycobacterium tuberculosis, is involved in heme degradation and iron utilization. The enzyme binds two stacked protoheme molecules per monomer. Unlike the canonical heme oxygenases, the enzyme does not release carbon monoxide or formaldehyde. Instead, it forms unique products, named mycobilins, that retain the alpha-meso-carbon at the ring cleavage site as an aldehyde group. EC
1.6.2.4 , NADPH-hemoprotein reductase, can act as electron donor in vitro.
History
EC 1.14.99.57 created 2017
Orthology
K21481 heme oxygenase (mycobilin-producing)
Genes
MTO : MTCTRI2_3657(TB11.2)
MTUB : MT7199_3655(TB11.2)
MDX : BTO20_04175 BTO20_34150
MBAI : MB901379_04491(hmoB)
MHEK : JMUB5695_00446(mhuD)
MKY : IWGMT90018_57870(TB11.2)
MPHL : MPHLCCUG_00457(mhuD)
MTHN : 4412656_04124(isdG)
MFLV : NCTC10271_00429(isdG)
MSAL : DSM43276_00464(mhuD)
MTER : 4434518_03758(isdG)
CGL : Cgl2677(Cgl2677) Cgl2991(Cgl2991)
CGQ : CGLAR1_12845 CGLAR1_14340
CRL : NCTC7448_00724(isdG)
CUW : LH390_04035 LH390_11210
CGF : CGUA_03980(mhuD1) CGUA_05910(mhuD2)
BFV : C628_13260 C628_15075
NAD : NCTC11293_01195(isdG)
RCR : NCTC10994_02189(isdG)
GAM : GII34_03620 GII34_10995
GPD : GII33_10570 GII33_19045
SAMB : SAM23877_6981(mhuD)
SLE : sle_40240(sle_40240)
SXT : KPP03845_102566(mhuD)
PSEV : USB125703_01926(mhuD)
AUL : DCC27_002330 DCC27_011115
AIG : QDX25_01660 QDX25_11030
NAQU : ENKNEFLB_00316(mhuD)
FRE : Franean1_0912 Franean1_6639
ACTL : L3i22_011670 L3i22_011690
BALA : DSM104299_04844(mhuD)
SBAE : DSM104329_00316(mhuD)
» show all
Taxonomy
Reference
Authors
Chim N, Iniguez A, Nguyen TQ, Goulding CW
Title
Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis.
Journal
Sequence
Reference
Authors
Nambu S, Matsui T, Goulding CW, Takahashi S, Ikeda-Saito M
Title
A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO.
Journal
Reference
Authors
Graves AB, Morse RP, Chao A, Iniguez A, Goulding CW, Liptak MD
Title
Crystallographic and spectroscopic insights into heme degradation by Mycobacterium tuberculosis MhuD.
Journal
Sequence
Other DBs
LinkDB
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