KEGG ENZYME: 1.2.8.2

ENZYME: 1.2.8.2

Entry

EC 1.2.8.2                  Enzyme

Name

aldehyde dehydrogenase (FAD-independent);
aldehyde oxidase;
aldehyde oxidoreductase;
Mop;
AORDd

Class

Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With a flavin or flavoprotein as acceptor

Sysname

aldehyde:flavodoxin oxidoreductase (FAD-independent)

Reaction(IUBMB)

an aldehyde + H2O + flavodoxin = a carboxylate + reduced flavodoxin [RN:R13670]

Reaction(KEGG)

R13670

Substrate

aldehyde [CPD:C00071];
H2O [CPD:C00001];
flavodoxin

Product

carboxylate [CPD:C00060];
reduced flavodoxin [CPD:C02745]

Comment

The enzyme, best characterized from the sulfate-reducing bacterium Megalodesulfovibrio gigas, belongs to the xanthine oxidase family of enzymes. However, it lacks the FAD-binding domain typically found in members of this family. Instead, it transfers electrons to flavodoxin, which fulfills the role of the missing domain. The enzyme contains a molybdenum-molybdopterin-cytosine dinucleotide (MCD) cofactor and two types of [2Fe-2S] clusters per monomer.

History

EC 1.2.8.2 created 2004 as EC 1.2.99.7, transferred 2026 to EC 1.2.8.2

Orthology

K07469

aldehyde dehydrogenase (FAD-independent)

Genes

RAP:	RHOA_5093(mop)

SDL:

Sdel_1475

SMUL:

SMUL_2101

SHAL:

SHALO_1855

SULS:

Sdiek1_1939

SULJ:

SJPD1_1855

SULT:

FA592_01805

SULH:

NL930_04860

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

DFK:	ACF3NB_01045

DSB:	LN040_09470

DAMI:

ACEB74_04625

DELF:

DESU86_0678(mop)

DLG:	GTC18478_07700

DMA:

DMR_05980

DCB:	C3Y92_17455

SOLI:

ACP59X_22950

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

FUN:	YSD1_28180

DBA:

Dbac_1562

DOA:	AXF15_08755

DESU:

NLA06_06185

DRT:

Dret_1808

DPS:

DP0270

DLM:	DPPLL_06320(mop)

DGL:	LA52FAK_01450(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

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

DNS:	ACHOLT_18930

DESD:

AusDCA_3076

DOR:	Desor_1273 Desor_3016

DAI:	Desaci_2677 Desaci_2707

DMI:	Desmer_1171

DEHA:

AAH944_00885

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

DPK:	JCM17209_04920

DGI:	Desgi_0268 Desgi_0270 Desgi_2922 Desgi_3899

DESL:

ABDB91_01480

AWO:	Awo_c03890(mop1) Awo_c14980(mop3) Awo_c27190

AWI:	CHL1_002337

AMAJ:

ACIUZZ_12875

ACAG:

ACIZ62_11645

ROB:

CK5_22910

BYL:	A4V09_21845

BPRO:

PMF13cell1_01056(mop_1)

BCOC:

BLCOC_50120(mop)

BLAB:

EYS05_07740

BWX:	NQ550_01935

BMAS:

LK422_16310

AHAD:

FRZ06_04645 FRZ06_15440 FRZ06_15450

CFM:	BJL90_11360

GFE:	Gferi_19165

TEM:	JW646_03490

TGC:	L0P85_04810

TPET:

TPHSE_11600(mop)

TVT:	TVTCOM_11530(mop)

TEB:	T8CH_1499(mop)

THYR:

P4S50_08340

MSUE:

NXG62_07415

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)

SPAX:

SPX_12520(mop)

SMAW:

SMWOGL2_12930(mop_1)

SRHA:

SRRS_17290(mop)

SAEI:

SATMO3_20920(mop)

SSPR:

JCM13218_15600

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:8354279]

Authors

Romao MJ, Barata BA, Archer M, Lobeck K, Moura I, Carrondo MA, LeGall J, Lottspeich F, Huber R, Moura JJ.

Title

Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe-2S] centers.

Journal

Eur J Biochem 215:729-32 (1993)
DOI:10.1111/j.1432-1033.1993.tb18085.x

Reference

2 [PMID:8218223]

Authors

Barata BA, LeGall J, Moura JJ.

Title

Aldehyde oxidoreductase activity in Desulfovibrio gigas: in vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen.

Journal

Biochemistry 32:11559-68 (1993)
DOI:10.1021/bi00094a012

Reference

3 [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]

Reference

4 [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

5 [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

6 [PMID:11713686]

Authors

Rebelo JM, Dias JM, Huber R, Moura JJ, Romao MJ.

Title

Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 A.

Journal

J Biol Inorg Chem 6:791-800 (2001)
DOI:10.1007/s007750100255

Sequence

[dgg:DGI_0902]

Reference

7 [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

Authors

Krippahl L, Palma PN, Moura I, Moura JJG.

Title

Modelling the electron-transfer complex between aldehyde oxidoreductase and flavodoxin.

Journal

Eur J Inorg Chem 2006:3835-3840 (2006)

Other DBs

ExplorEnz - The Enzyme Database:

1.2.8.2

IUBMB Enzyme Nomenclature:

1.2.8.2

ExPASy - ENZYME nomenclature database:

1.2.8.2

BRENDA, the Enzyme Database:

1.2.8.2

LinkDB

DBGET integrated database retrieval system