KEGG   ENZYME: 1.2.99.7Help
Entry
EC 1.2.99.7                 Enzyme                                 

Name
aldehyde dehydrogenase (FAD-independent);
aldehyde oxidase;
aldehyde oxidoreductase;
Mop;
AORDd
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With unknown physiological acceptors
BRITE hierarchy
Sysname
aldehyde:acceptor oxidoreductase (FAD-independent)
Reaction(IUBMB)
an aldehyde + H2O + acceptor = a carboxylate + reduced acceptor [RN:R00544]
Reaction(KEGG)
Substrate
aldehyde [CPD:C00071];
H2O [CPD:C00001];
acceptor [CPD:C00028]
Product
carboxylate [CPD:C00060];
reduced acceptor [CPD:C00030]
Comment
Belongs to the xanthine oxidase family of enzymes. The enzyme from Desulfovibrio sp. contains a molybdenum-molybdopterin-cytosine dinucleotide (MCD) complex and two types of [2Fe-2S] cluster per monomer, but does not contain FAD.
History
EC 1.2.99.7 created 2004
Orthology
K07469  aldehyde oxidoreductase
Genes
BCEW: DM40_5295
BAM: Bamb_5751
BAC: BamMC406_5518
BDL: AK34_5296
BLAT: WK25_17150
BTEI: WS51_26525
RGU: A4W93_01525
SDL: Sdel_1475
SMUL: SMUL_2101
SHAL: SHALO_1855
SULJ: SJPD1_1855
GUR: Gura_0998
PCA: Pcar_0220
PPD: Ppro_1551
DVU: DVU1559(mop)
DVL: Dvul_1574
DVM: DvMF_0641
DDE: Dde_3539
DDS: Ddes_1823
DMA: DMR_05980
DHY: DESAM_20433(mop)
DGG: DGI_0902(mop)
DPI: BN4_11183 BN4_11879(mop)
PPRF: DPRO_1126(mop)
DBA: Dbac_1562
DRT: Dret_1808
DPS: DP0270
DSF: UWK_01309
DAT: HRM2_07080(mop1) HRM2_38770(mop2)
DTO: TOL2_C39330(mop)
HOH: Hoch_4147
SFU: Sfum_1310
MHUA: MCHK_5950
AMIH: CO731_00453(mop)
MET: M446_1983
MNO: Mnod_1247
RBM: TEF_05295
RID: RIdsm_05003(mop)
ROH: FIU89_19770(mop)
EFL: EF62_2740
EFS: EFS1_2048
EFQ: DR75_1278
ENE: ENT_17490
CLS: CXIVA_04850(CoxL)
CSR: Cspa_c06890(mop1)
CSQ: CSCA_3243
CTYK: CTK_C17200
CDY: F3K33_02770(xdh)
RUM: CK1_27440
CCT: CC1_17680
ROB: CK5_22910
RTO: RTO_09230
BPRO: PMF13cell1_01056(mop_1)
LUA: D4A81_03745(xdh)
PDC: CDIF630_03469(xdhA5)
CDC: CD196_2987(xdhA3)
CDL: CDR20291_3033(xdhA3)
DHD: Dhaf_3146
DAE: Dtox_3440
PTH: PTH_0679
ELM: ELI_2450
EMT: CPZ25_004590(xdh)
AWO: Awo_c03890(mop1) Awo_c14980(mop3) Awo_c27190
OVA: OBV_43650(mop)
MED: MELS_0607
PFT: JBW_01067
STED: SPTER_09650(mop)
BHY: BHWA1_00070(coxL)
BRM: Bmur_2657
BPJ: B2904_orf2108(coxL)
BPW: WESB_2048(coxL)
BIP: Bint_1931
FUL: C4N20_09745(xdh)
FMO: C4N19_00290(xdh)
BLQ: L21SP5_02720(mop)
 » show all
Taxonomy
Reference
1  [PMID:14659539]
  Authors
Uchida H, Kondo D, Yamashita A, Nagaosa Y, Sakurai T, Fujii Y, Fujishiro K, Aisaka K, Uwajima T.
  Title
Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690.
  Journal
FEMS Microbiol Lett 229:31-6 (2003)
DOI:10.1016/S0378-1097(03)00781-X
Reference
2  [PMID:10679276]
  Authors
Duarte RO, Archer M, Dias JM, Bursakov S, Huber R, Moura I, Romao MJ, Moura JJ.
  Title
Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774.
  Journal
Biochem Biophys Res Commun 268:745-9 (2000)
DOI:10.1006/bbrc.2000.2135
Reference
3  [PMID:10727945]
  Authors
Andrade SL, Brondino CD, Feio MJ, Moura I, Moura JJ.
  Title
Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491 EPR assignment of the proximal [2Fe-2S] cluster to the Mo site.
  Journal
Eur J Biochem 267:2054-61 (2000)
DOI:10.1046/j.1432-1327.2000.01209.x
Reference
4  [PMID:7502041]
  Authors
Romao MJ, Archer M, Moura I, Moura JJ, LeGall J, Engh R, Schneider M, Hof P, Huber R.
  Title
Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas.
  Journal
Science 270:1170-6 (1995)
DOI:10.1126/science.270.5239.1170
  Sequence
[dgg:DGI_0902]
Other DBs
ExplorEnz - The Enzyme Database: 1.2.99.7
IUBMB Enzyme Nomenclature: 1.2.99.7
ExPASy - ENZYME nomenclature database: 1.2.99.7
BRENDA, the Enzyme Database: 1.2.99.7

DBGET integrated database retrieval system