KEGG ENZYME: 1.2.99.7

ENZYME: 1.2.99.7

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

Sysname

aldehyde:acceptor oxidoreductase (FAD-independent)

Reaction(IUBMB)

an aldehyde + H2O + acceptor = a carboxylate + reduced acceptor [RN:R00544]

Reaction(KEGG)

R00544 > R00638

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

RAP:	RHOA_5093(mop)

SDL:

Sdel_1475

SMUL:

SMUL_2101

SHAL:

SHALO_1855

SULS:

Sdiek1_1939

SULJ:

SJPD1_1855

SULT:

FA592_01805

GUR:

Gura_0998

PCA:

Pcar_0220

PACE:

A6070_10775 A6070_14425

PEF:	A7E78_09400

PPD:

Ppro_1551

DDS:

Ddes_1823

DFI:	AXF13_03440

DPG:	DESPIGER_0125

DEF:	CNY67_03300

DSB:	LN040_09470

DMA:

DMR_05980

DCB:	C3Y92_17455

DGG:	DGI_0902(mop)

DDE:

Dde_3539

DMS:	E8L03_03670 E8L03_11880

DSA:	Desal_0299

DHY:	DESAM_20433(mop)

DAF:	Desaf_0413

DPI:	BN4_11879(mop)

DEJ:	AWY79_13680

PPRF:

DPRO_1126(mop)

PSEL:

GM415_09125 GM415_15685

DDN:	DND132_0141

PSEF:

PSDVSF_12880(mop)

PPOR:

JCM14722_31400(mop)

PNW:	SYK_13630(mop_1) SYK_22350(mop_2)

PTHE:

LF599_07025 LF599_12100

PMEN:

V8V93_10045

DSX:	GD604_04725

DSD:	GD606_04460

PBIZ:

LWC08_01190

DVU:	DVU_1559(mop)

DVL:

Dvul_1574

DVM:

DvMF_0641

DVG:	Deval_1735

CLIH:

KPS_000767

BWS:	WCP94_003305 WCP94_004447

DBA:

Dbac_1562

DOA:	AXF15_08755

DESU:

NLA06_06185

DRT:

Dret_1808

DPS:

DP0270

DLM:	DPPLL_06320(mop)

DPR:	Despr_1636

DEO:	CAY53_03230 CAY53_03300

DOG:	HP555_04800

DAT:	HRM2_07080(mop1) HRM2_38770(mop2)

DTO:	TOL2_C39330(mop)

DHG:	EYB58_07105

DOV:	DSCO28_12970(mop_1) DSCO28_16460(mop_2) DSCO28_22590 DSCO28_54420(mop_3)

DWD:	DSCW_31270(mop) DSCW_61540

DALK:

DSCA_49590(mop)

DVR:	Dvar_13480 Dvar_59630 Dvar_62190 Dvar_79330

DLI:

dnl_22250

DTI:	Desti_0720 Desti_1799

SFU:

Sfum_1310

DMP:

FAK_32330

ALIC:

GI364_09355

CLJ:	CLJU_c24050 CLJU_c24130

CLS:	CXIVA_04850(CoxL)

CSR:	Cspa_c06890(mop1)

CAH:	CAETHG_0471

CSQ:

CSCA_3243

CCK:	Ccar_24780

CTYK:

CTK_C17200

CEU:	A7L45_05835

CFM:	BJL90_11360

CDRK:

B9W14_03710

CLOS:

DMR38_12345 DMR38_12385

CGEL:

psyc5s11_25370

RUM:

CK1_27440

RGV:	NQ502_15120 NQ502_17970

OVA:	OBV_43650(mop)

PETR:

QKW49_07245 QKW49_23100

DSY:	DSY0872 DSY1987

DHD:

Dhaf_3146

DDH:	Desde_2603

DOR:	Desor_1273 Desor_3016

DAI:	Desaci_2677 Desaci_2707

DMI:	Desmer_1171

DCA:	Desca_1570

PTH:

PTH_0679

DRU:	Desru_0522

DFG:	B0537_02740

DAE:

Dtox_3440

FWA:	DCMF_02040 DCMF_08470 DCMF_14090 DCMF_14115 DCMF_21835 DCMF_26870

DGI:	Desgi_0268 Desgi_0270 Desgi_2922 Desgi_3899

AWO:	Awo_c03890(mop1) Awo_c14980(mop3) Awo_c27190

AWI:	CHL1_002337

ROB:

CK5_22910

BYL:	A4V09_21845

BPRO:

PMF13cell1_01056(mop_1)

BLAB:

EYS05_07740

BWX:	NQ550_01935

BMAS:

LK422_16310

BCOC:

BLCOC_50120(mop)

AHAD:

FRZ06_04645 FRZ06_15440 FRZ06_15450

GFE:	Gferi_19165

TEM:	JW646_03490

TGC:	L0P85_04810

TPET:

TPHSE_11600(mop)

TEB:	T8CH_1499(mop)

THYR:

P4S50_08340

PFT:

JBW_01067

STED:

SPTER_09650(mop)

SSPH:

SPSPH_012610(mop)

SOVA:

SOV_19280(mop_1) SOV_19340(mop_2)

SSID:

SPSIL_006570(mop_1) SPSIL_024710(mop_2) SPSIL_030050(mop_3) SPSIL_034290(mop_4) SPSIL_036990(mop_5)

SACV:

SPACI_015430(mop_1) SPACI_015640(mop_2) SPACI_017230(mop_3)

FBS:	N510_000745(mop_1) N510_002966(mop_2)

CPOR:

BED41_02500 BED41_02975 BED41_11740

AMO:	Anamo_0983 Anamo_1057

ARAM:

KAR29_01710

APRP:

KIH16_01710

STR:	Sterm_3270

» show all

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]