KEGG   ENZYME: 1.14.99.58Help
Entry
EC 1.14.99.58               Enzyme                                 

Name
heme oxygenase (biliverdin-IX-beta and delta-forming);
pigA (gene name)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous
BRITE hierarchy
Sysname
protoheme,donor:oxygen oxidoreductase (biliverdin-IX-beta and delta-forming)
Reaction(IUBMB)
(1) protoheme + 3 reduced acceptor + 3 O2 = biliverdin-IX-delta + CO + Fe2+ + 3 acceptor + 3 H2O [RN:R11816];
(2) protoheme + 3 reduced acceptor + 3 O2 = biliverdin-IX-beta + CO + Fe2+ + 3 acceptor + 3 H2O [RN:R11817]
Reaction(KEGG)
Substrate
protoheme [CPD:C00032];
reduced acceptor [CPD:C00030];
O2 [CPD:C00007]
Product
biliverdin-IX-delta [CPD:C21723];
CO [CPD:C00237];
Fe2+ [CPD:C14818];
acceptor [CPD:C00028];
H2O [CPD:C00001];
biliverdin-IX-beta [CPD:C21724]
Comment
The enzyme, characterized from the bacterium Pseudomonas aeruginosa, differs from EC 1.14.15.20, heme oxygenase (biliverdin-producing, ferredoxin), in that the heme substrate is rotated by approximately 110 degrees within the active site, resulting in cleavage at a different part of the ring. It forms a mixture of about 70% biliverdin-IX-delta and 30% biliverdin-IX-beta.
History
EC 1.14.99.58 created 2017
Pathway
ec00860  Porphyrin and chlorophyll metabolism
Orthology
K07215  heme oxygenase (biliverdin-IX-beta and delta-forming)
Genes
XCC: XCC4155
XCB: XC_4242
XCA: xcc-b100_4369
XCP: XCR_4490
XCV: XCV4393
XAX: XACM_4166
XAC: XAC4294
XCI: XCAW_04660
XCT: J151_04476
XCJ: J158_04427
XOM: XOO0263(XOO0263)
XOO: XOO0291(HemO)
XOP: PXO_03309
XOR: XOC_0227
XAL: XALC_3120
XPH: XppCFBP6546_12755(XppCFBP6546P_12755)
SML: Smlt3896(pigA)
SMT: Smal_3312
SMZ: SMD_3498(hemO)
PAE: PA0672(hemO)
PAEV: N297_691
PAEI: N296_691
PAU: PA14_55580(nemO)
PAG: PLES_46571(hemO)
PAF: PAM18_4366(hemO)
PNC: NCGM2_1335(nemO)
PAEB: NCGM1900_2097(nemO)
PAEP: PA1S_23245
PAEM: U769_23030
PAEL: T223_23770
PAEG: AI22_10820
PAEC: M802_689
PAEO: M801_691
PMY: Pmen_4507
PMK: MDS_0284
PPU: PP_1005(hemO) PP_2582
PPT: PPS_1032
PPUH: B479_05305
PPUN: PP4_32840 PP4_43110(hemO)
PMON: X969_03390
PMOT: X970_03365
PSB: Psyr_1104
PSYR: N018_20130
PFL: PFL_4628(hemO)
PPRO: PPC_4730(hemO)
PFE: PSF113_1273(hemO)
PFC: PflA506_4278(hemO)
PFB: VO64_1844
PSA: PST_4185
PSTT: CH92_21665
PKC: PKB_3153
PSES: PSCI_0686
PSEM: TO66_24120
PSOS: POS17_4695(hemO)
PANR: A7J50_4738
PSET: THL1_4048
PSIL: PMA3_23130
ABM: ABSDF2281(hemO)
ABN: AB57_0991
ABH: M3Q_1216
ABAZ: P795_13120
ABAU: IX87_00955
ACI: ACIAD1478(hemO)
AGU: AS4_16540(hemO) AS4_29790(hemO) AS4_34070(hemO)
AUG: URS_0079
MCT: MCR_0810
MCS: DR90_1063(hemO)
SDN: Sden_0219
PSPO: PSPO_b1580(hemO)
CJA: CJA_2682
MEJ: Q7A_2860
AEH: Mlg_1496
TVR: TVD_09365
AXE: P40_13405
NME: NMB1669
NMP: NMBB_1917
NMA: NMA1927
NMW: NMAA_1385(hemO)
NMX: NMA510612_2169(hemO)
NMC: NMC1587(hemO)
NMN: NMCC_1580(hemO)
NMT: NMV_0703(hemO)
NMI: NMO_1487(hemO)
NGO: NGO1318
NGK: NGK_1541
NLA: NLA_6120(hemO)
LHK: LHK_02725
AMAH: DLM_2969
BGU: KS03_4065
BGO: BM43_6159
BYI: BYI23_A015060(bphO)
BUE: BRPE67_ACDS15560(bphO)
BFN: OI25_4917
CABA: SBC2_20550
AAV: Aave_2977
AAA: Acav_2319
CTES: O987_09790
RTA: Rta_25460
HSE: Hsero_4544(hemO)
HRB: Hrubri_4500(hemO)
MEP: MPQ_1657(hemO)
TCL: Tchl_2218
DGG: DGI_2596
CCX: COCOR_00945(bphO)
SUR: STAUR_7007(bphO)
HOH: Hoch_4727
ATU: Atu2502(hemO)
ATF: Ach5_23710(hemO)
AVI: Avi_3495
AGR: AGROH133_08500(hemO)
REC: RHECIAT_CH0003530(bphO)
RLE: RL3713
RLG: Rleg_3288
RIR: BN877_I2583(hemO)
RHT: NT26_1760
NEN: NCHU2750_34870(hemO)
OAH: DR92_4615
BBT: BBta_2329
BRS: S23_54790
AOL: S58_55370
RPA: RPA3279(pigA)
RPT: Rpal_3698
OCA: OCAR_4136
XAU: Xaut_2445
AZC: AZC_2040
MDI: METDI5077
MEX: Mext_4082
MCH: Mchl_4450
MPO: Mpop_4563
MET: M446_0885
MOR: MOC_4248(bphO)
META: Y590_20350
MAQU: Maq22A_c21180(hemO)
MSL: Msil_2021
HDN: Hden_2796
BVR: BVIR_2196
BLAG: BLTE_19160(hemO)
MMED: Mame_00817
PZU: PHZ_c2262
RSP: RSP_4190
LAQU: R2C4_20575
CID: P73_1096
RHC: RGUI_1106
STAX: MC45_16995
SSAN: NX02_26430
SPMI: K663_02750
SPHR: BSY17_1837
SINB: SIDU_13215
SPHT: K426_18055
AAY: WYH_02835
ALB: AEB_P0666
GOX: GOX0243
GXL: H845_716
APK: APA386B_225(pigA)
ASZ: ASN_1866(pigA) ASN_3570(pigA)
RCE: RC1_0553
MGRY: MSR1_18660
MAGX: XM1_4194
TXI: TH3_20460
FAL: FRAAL5335
GOB: Gobs_1420
MMAR: MODMU_1429
KRA: Krad_1985
DGO: DGo_CA1219(bphO)
DFC: DFI_17940
ACA: ACP_0892
ABAS: ACPOL_3586
CPI: Cpin_7208
FLN: FLA_1968
PHE: Phep_3915
DFE: Dfer_3184
SLI: Slin_0385
FAE: FAES_0304(bphO)
HSW: Hsw_3265
FJO: Fjoh_3937
ZPR: ZPR_2283
DDO: I597_2677
CHZ: CHSO_3896(bphO)
MESQ: C7H62_2350
FBA: FIC_02098
NMG: Nmag_4071
 » show all
Taxonomy
Reference
1  [PMID:11591684]
  Authors
Ratliff M, Zhu W, Deshmukh R, Wilks A, Stojiljkovic I
  Title
Homologues of neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa.
  Journal
J Bacteriol 183:6394-403 (2001)
DOI:10.1128/JB.183.21.6394-6403.2001
Reference
2  [PMID:12475329]
  Authors
Caignan GA, Deshmukh R, Wilks A, Zeng Y, Huang HW, Moenne-Loccoz P, Bunce RA, Eastman MA, Rivera M
  Title
Oxidation of heme to beta- and delta-biliverdin by Pseudomonas aeruginosa heme oxygenase as a consequence of an unusual seating of the heme.
  Journal
J Am Chem Soc 124:14879-92 (2002)
DOI:10.1021/ja0274960
Reference
3  [PMID:15122889]
  Authors
Friedman J, Lad L, Li H, Wilks A, Poulos TL
  Title
Structural basis for novel delta-regioselective heme oxygenation in the opportunistic pathogen Pseudomonas aeruginosa.
  Journal
Biochemistry 43:5239-45 (2004)
DOI:10.1021/bi049687g
  Sequence
[pae:PA0672]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.99.58
IUBMB Enzyme Nomenclature: 1.14.99.58
ExPASy - ENZYME nomenclature database: 1.14.99.58
BRENDA, the Enzyme Database: 1.14.99.58

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