P29082 (SOR_ACIAM) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sulfur oxygenase/reductase
EC=1.13.11.55

Alternative name(s):
Sulfur oxygenase reductase
Short name=SOR

Gene names

Name:

sor

Organism

Acidianus ambivalens (Desulfurolobus ambivalens)

Taxonomic identifier

2283 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Acidianus

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products. Ref.2
Catalytic activity	4 sulfur + 4 H2O + O2 = 2 H2S + 2 HSO3- + 2 H+.
Cofactor	Binds 1 iron ion per subunit. Ref.2
Enzyme regulation	Inhibited by zinc. Ref.2
Subunit structure	Homoicosatetramer. The resulting structure is a hollow sphere where catalysis takes place in the inside cavity. Ref.2 Ref.4
Subcellular location	Cytoplasm.
Induction	Aerobically induced. Ref.2
Biophysicochemical properties	Kinetic parameters: KM=23 mM for sulfur (at 65 degrees Celsius, with the oxygenase reaction) Ref.2 KM=13 mM for sulfur (at 65 degrees Celsius, with the reductase reaction)

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sulfur oxygenase/reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 309

308

Sulfur oxygenase/reductase

PRO_0000072042

Sites

Metal binding

86

1

Iron; via tele nitrogen

Metal binding

90

1

Iron; via tele nitrogen

Metal binding

114

1

Iron

Amino acid modifications

Modified residue

31

1

Cysteine persulfide

Experimental info

Mutagenesis

31

1

C → A or S: No enzyme activity. Still binds iron. Ref.3

Mutagenesis

86

1

H → A: No enzyme activity and no iron bound. Ref.3

Mutagenesis

90

1

H → A: No enzyme activity and no iron bound. Ref.3

Mutagenesis

101

1

C → A: 10% residual activity. Ref.3

Mutagenesis

101

1

C → S: 1% residual enzyme activity, and no iron bound. Ref.3

Mutagenesis

104

1

C → A or S: 10% residual activity. Ref.3

Mutagenesis

114

1

E → A: No enzyme activity and no iron bound. Ref.3

Mutagenesis

114

1

E → D: 1% residual enzyme activity and 4% of wild-type levels of iron bound. Ref.3

Secondary structure

1

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309

Helix Strand Turn

Details...

Beta strand

5 – 14

10

Helix

17 – 34

18

Beta strand

40 – 51

12

Turn

54 – 60

7

Turn

66 – 68

3

Beta strand

70 – 82

13

Helix

83 – 92

10

Helix

94 – 102

9

Helix

103 – 107

5

Beta strand

108 – 113

6

Beta strand

115 – 123

9

Turn

130 – 132

3

Helix

133 – 142

10

Helix

146 – 148

3

Beta strand

156 – 168

13

Helix

173 – 187

15

Beta strand

193 – 204

12

Turn

206 – 210

5

Helix

214 – 221

8

Beta strand

225 – 227

3

Helix

231 – 233

3

Helix

239 – 241

3

Beta strand

244 – 256

13

Helix

257 – 269

13

Helix

271 – 281

11

Beta strand

284 – 299

16

Helix

302 – 307

6

Sequences

	Sequence		Length	Mass (Da)
	P29082 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 95C0EEBF0AD079A6	FASTA	309	35,318
	10 20 30 40 50 60 MPKPYVAINM AELKNEPKTF EMFASVGPKV CMVTARHPGF VGFQNHIQIG ILPFGNRYGG 70 80 90 100 110 120 AKMDMTKESS TVRVLQYTFW KDWKDHEEMH RQNWSYLFRL CYSCASQMIW GPWEPIYEII 130 140 150 160 170 180 YANMPINTEM TDFTAVVGKK FAEGKPLDIP VISQPYGKRV VAFAEHSVIP GKEKQFEDAI 190 200 210 220 230 240 VRTLEMLKKA PGFLGAMVLK EIGVSGIGSM QFGAKGFHQV LENPGSLEPD PNNVMYSVPE 250 260 270 280 290 300 AKNTPQQYIV HVEWANTDAL MFGMGRVLLY PELRQVHDEV LDTLVYGPYI RILNPMMEGT FWREYLNEQ

References

[1]	"Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus ambivalens." Kletzin A. J. Bacteriol. 174:5854-5859(1992) [PubMed: 1522063] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-29. Strain: Lei 10 / DSM 3772 / JCM 9191.
[2]	"The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre." Urich T., Bandeiras T.M., Leal S.S., Rachel R., Albrecht T., Zimmermann P., Scholz C., Teixeira M., Gomes C.M., Kletzin A. Biochem. J. 381:137-146(2004) [PubMed: 15030315] [Abstract] Cited for: FUNCTION, CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, SUBUNIT.
[3]	"Identification of core active site residues of the sulfur oxygenase reductase from Acidianus ambivalens by site-directed mutagenesis." Urich T., Kroke A., Bauer C., Seyfarth K., Reuff M., Kletzin A. FEMS Microbiol. Lett. 248:171-176(2005) [PubMed: 15970399] [Abstract] Cited for: MUTAGENESIS OF CYS-31; HIS-86; HIS-90; CYS-101; CYS-104 AND GLU-114.
[4]	"X-ray structure of a self-compartmentalizing sulfur cycle metalloenzyme." Urich T., Gomes C.M., Kletzin A., Frazao C. Science 311:996-1000(2006) [PubMed: 16484493] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH IRON, SUBUNIT, PERSULFURATION AT CYS-31, REACTION MECHANISM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X56616 Genomic DNA. Translation: CAA39952.1.

PIR

B43331.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CB2	X-ray	1.70	A/B/C/D/E/F	1-309	[»]

ProteinModelPortal

P29082.

SMR

P29082. Positions 2-308.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-12389.

BRENDA

1.13.11.55. 86.

Family and domain databases

InterPro

IPR011008. Dimeric_a/b-barrel.
IPR011661. S_Oase_red.
[Graphical view]

Pfam

PF07682. SOR. 1 hit.
[Graphical view]

SUPFAM

SSF54909. Dimer_A_B_barrel. 1 hit.

ProtoNet

Search...

Entry information

Entry name

SOR_ACIAM

Accession

Primary (citable) accession number: P29082

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 28, 2011
This is version 61 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program