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1. Oxidoreductases

1.8 Acting on a sulfur group of donors

1.8.99 With unknown physiological acceptors

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UniProtKB Enzyme Link:	UniProtKB 1.8.99.2
BRENDA Enzyme Link:	BRENDA 1.8.99.2
KEGG Enzyme Link:	KEGG1.8.99.2
BioCyc Enzyme Link:	BioCyc 1.8.99.2
ExPASy Enzyme Link:	ExPASy1.8.99.2
EC2PDB Enzyme Link:	EC2PDB 1.8.99.2
ExplorEnz Enzyme Link:	ExplorEnz 1.8.99.2
PRIAM enzyme-specific profiles Link:	PRIAM 1.8.99.2
IntEnz Enzyme Link:	IntEnz 1.8.99.2
MEDLINE Enzyme Link:	MEDLINE 1.8.99.2

RHEA:24240	A + AMP + 2 H(+) + sulfite = adenosine 5'-phosphosulfate + AH2
RULE(radius=1)	[:1]-[OH;+0:2].[:3]=[S;H0;+0:4](-[:5])-[OH;+0:6].[H+;H0:7].[H+;H0:8]>>[:3]=[S;H0;+0:4](-[:5])(=[O;H0;+0:6])-[O;H0;+0:2]-[:1]
Reaction
Core-to-Core	No scaffolds atoms were exchanged as a result of the reaction

Title	Authors	Date	PubMed ID
Localization of dehydrogenases, reductases, and electron transfer components in the sulfate-reducing bacterium Desulfovibrio gigas.	Odom JM, Peck HD Jr	1981 Jul	7240092
A flavin-sulfite adduct as an intermediate in the reaction catalyzed by adenylyl sulfate reductase from Desulfovibrio vulgaris.	Michaels GB, Davidson JT, Peck HD Jr	1970 May 11	5421934
The active centers of adenylylsulfate reductase from Desulfovibrio gigas. Characterization and spectroscopic studies.	Lampreia J, Moura I, Teixeira M, Peck HD Jr, Legall J, Huynh BH, Moura JJ	1990 Mar 30	2158885
Crystal structure of Adenylylsulfate reductase from Desulfovibrio gigas suggests a potential self-regulation mechanism involving the C terminus of the beta-subunit.	Chiang YL, Hsieh YC, Fang JY, Liu EH, Huang YC, Chuankhayan P, Jeyakanthan J, Liu MY, Chan SI, Chen CJ	2009 Dec	19820092