P80564 (PGTS_PELAC) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyrogallol hydroxytransferase small subunit
EC=1.97.1.2

Alternative name(s):
Transhydroxylase subunit beta

Gene names

Name:

bthL

Organism

Pelobacter acidigallici

Taxonomic identifier

35816 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfuromonadales › Pelobacteraceae › Pelobacter

Protein attributes

Sequence length	274 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Isomerization of pyrogallol to phloroglucin.
Catalytic activity	1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene.
Cofactor	Binds 3 4Fe-4S clusters.
Subunit structure	Heterodimer of a large and a small subunit.

Ontologies

Keywords
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyrogallol hydroxytransferase 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

Chain

1 – 274

274

Pyrogallol hydroxytransferase small subunit

PRO_0000058366

Sites

Metal binding

13

1

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

16

1

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

19

1

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

23

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

68

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

71

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

76

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

109

1

Iron-sulfur 3 (4Fe-4S) By similarity

Metal binding

126

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

129

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

145

1

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

149

1

Iron-sulfur 1 (4Fe-4S) By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

274

Helix Strand Turn

Details...

Beta strand

3 – 9

7

Helix

10 – 12

3

Helix

18 – 27

10

Turn

33 – 35

3

Beta strand

45 – 54

10

Beta strand

60 – 66

7

Helix

75 – 79

5

Turn

80 – 82

3

Beta strand

83 – 86

4

Beta strand

92 – 94

3

Turn

96 – 101

6

Helix

103 – 108

6

Beta strand

115 – 117

3

Turn

118 – 121

4

Beta strand

122 – 124

3

Helix

130 – 133

4

Helix

144 – 148

5

Beta strand

154 – 159

6

Helix

161 – 171

11

Helix

178 – 180

3

Beta strand

185 – 190

6

Helix

192 – 195

4

Beta strand

197 – 205

9

Beta strand

214 – 219

6

Beta strand

222 – 228

7

Beta strand

233 – 240

8

Beta strand

242 – 251

10

Beta strand

254 – 265

12

Beta strand

267 – 274

8

Sequences

	Sequence		Length	Mass (Da)
	P80564 [UniParc]. Last modified January 16, 2004. Version 2. Checksum: 2F9A9CD24082F5A1	FASTA	274	31,221
	10 20 30 40 50 60 MEQYYMVIDV AKCQDCNNCF MGCMDEHELN EWPGYTASMQ RGHRWMNIER RERGTYPRND 70 80 90 100 110 120 INYRPTPCMH CENAPCVAKG NGAVYQREDG IVLIDPEKAK GKKELLDTCP YGVMYWNEEE 130 140 150 160 170 180 NVAQKCTMCA HLLDDESWAP KMPRCAHNCG SFVYEFLKTT PEAMAKKVEE EGLEVIKPEL 190 200 210 220 230 240 GTKPRVYYKN LYRFEKNYVT AGILVQGDCF EGAKVVLKSG GKEVASAETN FFGEFKFDAL 250 260 270 DNGEYTVEID ADGKSYSDTV VIDDKSVDLG FIKL

References

[1]	Retey J. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"One molecule of molybdopterin guanine dinucleotide is associated with each subunit of the heterodimeric Mo-Fe-S protein transhydroxylase of Pelobacter acidigallici as determined by SDS/PAGE and mass spectrometry." Reichenbecher W., Ruediger A., Kroneck P.M.H., Schink B. Eur. J. Biochem. 237:406-413(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15. Strain: DSM 2377 / Braunschweig.
[3]	"Towards the reaction mechanism of pyrogallol-phloroglucinol transhydroxylase of Pelobacter acidigallici." Reichenbecher W., Schink B. Biochim. Biophys. Acta 1430:245-253(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ243850 Genomic DNA. Translation: CAB50914.1.

PIR

S65429.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TI2	X-ray	2.35	B/D/F/H/J/L	1-274	[»]
1TI4	X-ray	2.20	B/D/F/H/J/L	1-274	[»]
1TI6	X-ray	2.00	B/D/F/H/J/L	1-274	[»]
1VLD	X-ray	2.35	N/P/R/T/V/X	1-274	[»]
1VLE	X-ray	2.20	N/P/R/T/V/X	1-274	[»]
1VLF	X-ray	2.00	N/P/R/T/V/X	1-274	[»]

ProteinModelPortal

P80564.

SMR

P80564. Positions 1-274.

ModBase

Search...

Protein family/group databases

TCDB

5.A.3.7.1. prokaryotic molybdopterin-containing oxidoreductase (PMO) family.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.40.10. 1 hit.

InterPro

IPR017896. 4Fe4S_Fe-S-bd.
IPR008454. Collagen-bd_Cna-like_B-typ_dom.
IPR008970. Collagen-bd_Cna_B-typ_dom.
IPR013783. Ig-like_fold.
[Graphical view]

Pfam

PF05738. Cna_B. 1 hit.
PF13247. Fer4_11. 1 hit.
[Graphical view]

SUPFAM

SSF49478. Cna_B_unit. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P80564.

Entry information

Entry name

PGTS_PELAC

Accession

Primary (citable) accession number: P80564
Secondary accession number(s): Q9XAY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 16, 2004
Last modified:	April 3, 2013
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program