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P80563

- PGTL_PELAC

UniProt

P80563 - PGTL_PELAC

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Protein

Pyrogallol hydroxytransferase large subunit

Gene

athL

Organism
Pelobacter acidigallici
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Isomerisation of pyrogallol to phloroglucin.

Catalytic activityi

1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene.

Cofactori

Mo-bis(molybdopterin guanine dinucleotide)1 PublicationNote: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi175 – 1751Molybdenum

GO - Molecular functioni

  1. molybdenum ion binding Source: InterPro
  2. pyrogallol hydroxytransferase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Molybdenum

Protein family/group databases

TCDBi5.A.3.7.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyrogallol hydroxytransferase large subunit (EC:1.97.1.2)
Alternative name(s):
Transhydroxylase subunit alpha
Gene namesi
Name:athL
OrganismiPelobacter acidigallici
Taxonomic identifieri35816 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 875874Pyrogallol hydroxytransferase large subunitPRO_0000063242Add
BLAST

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.1 Publication

Structurei

Secondary structure

1
875
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Beta strandi16 – 216Combined sources
Beta strandi24 – 296Combined sources
Turni35 – 373Combined sources
Beta strandi44 – 463Combined sources
Beta strandi49 – 513Combined sources
Helixi61 – 644Combined sources
Helixi67 – 704Combined sources
Beta strandi73 – 753Combined sources
Beta strandi80 – 823Combined sources
Helixi93 – 953Combined sources
Helixi98 – 1014Combined sources
Helixi105 – 1084Combined sources
Beta strandi109 – 1113Combined sources
Helixi114 – 13118Combined sources
Helixi134 – 1363Combined sources
Beta strandi137 – 1404Combined sources
Turni149 – 1513Combined sources
Turni153 – 1553Combined sources
Helixi156 – 1649Combined sources
Beta strandi167 – 1704Combined sources
Turni174 – 1763Combined sources
Helixi177 – 1815Combined sources
Helixi183 – 1875Combined sources
Helixi190 – 1923Combined sources
Helixi201 – 2088Combined sources
Beta strandi210 – 2167Combined sources
Helixi219 – 2224Combined sources
Beta strandi224 – 2263Combined sources
Turni228 – 2314Combined sources
Helixi232 – 2409Combined sources
Beta strandi244 – 2485Combined sources
Helixi254 – 2596Combined sources
Beta strandi261 – 2644Combined sources
Helixi271 – 28414Combined sources
Helixi290 – 2967Combined sources
Beta strandi297 – 2993Combined sources
Helixi300 – 3078Combined sources
Turni308 – 3125Combined sources
Helixi318 – 3258Combined sources
Helixi329 – 34113Combined sources
Beta strandi344 – 3485Combined sources
Turni349 – 3524Combined sources
Helixi356 – 3583Combined sources
Helixi363 – 37614Combined sources
Turni377 – 3804Combined sources
Beta strandi389 – 3913Combined sources
Helixi404 – 4063Combined sources
Turni408 – 4103Combined sources
Turni413 – 4153Combined sources
Helixi417 – 4193Combined sources
Helixi422 – 4265Combined sources
Beta strandi429 – 4313Combined sources
Beta strandi438 – 4414Combined sources
Beta strandi446 – 4483Combined sources
Helixi449 – 4513Combined sources
Helixi452 – 4587Combined sources
Beta strandi461 – 4644Combined sources
Helixi475 – 4773Combined sources
Beta strandi479 – 4835Combined sources
Beta strandi492 – 4976Combined sources
Helixi500 – 5034Combined sources
Beta strandi504 – 5063Combined sources
Helixi508 – 5136Combined sources
Beta strandi521 – 5299Combined sources
Helixi533 – 5353Combined sources
Beta strandi537 – 5426Combined sources
Helixi545 – 5473Combined sources
Beta strandi550 – 5534Combined sources
Helixi564 – 5674Combined sources
Beta strandi568 – 5703Combined sources
Beta strandi572 – 5765Combined sources
Helixi589 – 59911Combined sources
Helixi603 – 6075Combined sources
Helixi612 – 62110Combined sources
Helixi625 – 6273Combined sources
Helixi631 – 6377Combined sources
Beta strandi639 – 6413Combined sources
Beta strandi646 – 6483Combined sources
Helixi655 – 6584Combined sources
Helixi672 – 6743Combined sources
Beta strandi686 – 6916Combined sources
Helixi693 – 7008Combined sources
Turni721 – 7233Combined sources
Helixi725 – 7284Combined sources
Beta strandi732 – 7354Combined sources
Beta strandi746 – 7494Combined sources
Helixi753 – 7564Combined sources
Turni758 – 7603Combined sources
Beta strandi761 – 7644Combined sources
Beta strandi767 – 7759Combined sources
Helixi776 – 7816Combined sources
Beta strandi789 – 7946Combined sources
Beta strandi797 – 80913Combined sources
Beta strandi813 – 8153Combined sources
Beta strandi825 – 8284Combined sources
Turni829 – 8313Combined sources
Beta strandi834 – 8363Combined sources
Helixi839 – 8413Combined sources
Beta strandi848 – 8514Combined sources
Beta strandi860 – 8667Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TI2X-ray2.35A/C/E/G/I/K1-875[»]
1TI4X-ray2.20A/C/E/G/I/K1-875[»]
1TI6X-ray2.00A/C/E/G/I/K1-875[»]
1VLDX-ray2.35M/O/Q/S/U/W1-875[»]
1VLEX-ray2.20M/O/Q/S/U/W1-875[»]
1VLFX-ray2.00M/O/Q/S/U/W1-875[»]
ProteinModelPortaliP80563.
SMRiP80563. Positions 1-875.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80563.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
[Graphical view]
PfamiPF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80563-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGEVVRLTNS STGGPVFVYV KDGKIIRMTP MDFDDAVDAP SWKIEARGKT
60 70 80 90 100
FTPPRKTSIA PYTAGFKSMI YSDLRIPYPM KRKSFDPNGE RNPQLRGAGL
110 120 130 140 150
SKQDPWSDYE RISWDEATDI VVAEINRIKH AYGPSAILST PSSHHMWGNV
160 170 180 190 200
GYRHSTYFRF MNMMGFTYAD HNPDSWEGWH WGGMHMWGFS WRLGNPEQYD
210 220 230 240 250
LLEDGLKHAE MIVFWSSDPE TNSGIYAGFE SNIRRQWLKD LGVDFVFIDP
260 270 280 290 300
HMNHTARLVA DKWFSPKIGT DHALSFAIAY TWLKEDSYDK EYVAANAHGF
310 320 330 340 350
EEWADYVLGK TDGTPKTCEW AEEESGVPAC EIRALARQWA KKNTYLAAGG
360 370 380 390 400
LGGWGGACRA SHGIEWARGM IALATMQGMG KPGSNMWSTT QGVPLDYEFY
410 420 430 440 450
FPGYAEGGIS GDCENSAAGF KFAWRMFDGK TTFPSPSNLN TSAGQHIPRL
460 470 480 490 500
KIPECIMGGK FQWSGKGFAG GDISHQLHQY EYPAPGYSKI KMFWKYGGPH
510 520 530 540 550
LGTMTATNRY AKMYTHDSLE FVVSQSIWFE GEVPFADIIL PACTNFERWD
560 570 580 590 600
ISEFANCSGY IPDNYQLCNH RVISLQAKCI EPVGESMSDY EIYRLFAKKL
610 620 630 640 650
NIEEMFSEGK DELAWCEQYF NATDMPKYMT WDEFFKKGYF VVPDNPNRKK
660 670 680 690 700
TVALRWFAEG REKDTPDWGP RLNNQVCRKG LQTTTGKVEF IATSLKNFEE
710 720 730 740 750
QGYIDEHRPS MHTYVPAWES QKHSPLAVKY PLGMLSPHPR FSMHTMGDGK
760 770 780 790 800
NSYMNYIKDH RVEVDGYKYW IMRVNSIDAE ARGIKNGDLI RAYNDRGSVI
810 820 830 840 850
LAAQVTECLQ PGTVHSYESC AVYDPLGTAG KSADRGGCIN ILTPDRYISK
860 870
YACGMANNTA LVEIEKWDGD KYEIY
Length:875
Mass (Da):99,261
Last modified:January 23, 2007 - v3
Checksum:iB5D7DE5FAEF53A61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243850 Genomic DNA. Translation: CAB50913.1.
PIRiS65430.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243850 Genomic DNA. Translation: CAB50913.1 .
PIRi S65430.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TI2 X-ray 2.35 A/C/E/G/I/K 1-875 [» ]
1TI4 X-ray 2.20 A/C/E/G/I/K 1-875 [» ]
1TI6 X-ray 2.00 A/C/E/G/I/K 1-875 [» ]
1VLD X-ray 2.35 M/O/Q/S/U/W 1-875 [» ]
1VLE X-ray 2.20 M/O/Q/S/U/W 1-875 [» ]
1VLF X-ray 2.00 M/O/Q/S/U/W 1-875 [» ]
ProteinModelPortali P80563.
SMRi P80563. Positions 1-875.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

TCDBi 5.A.3.7.1. the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P80563.

Family and domain databases

InterProi IPR009010. Asp_de-COase-like_dom.
IPR006657. MoPterin_dinucl-bd_dom.
IPR006656. Mopterin_OxRdtase.
[Graphical view ]
Pfami PF00384. Molybdopterin. 1 hit.
PF01568. Molydop_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
ProtoNeti Search...

Publicationsi

  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 2-17.
    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.
  4. "Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols."
    Messerschmidt A., Niessen H., Abt D., Einsle O., Schink B., Kroneck P.M.
    Proc. Natl. Acad. Sci. U.S.A. 101:11571-11576(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-874 IN COMPLEXES WITH MO-BIS-MGD; SUBSTRATE OR INHIBITOR AND THE SMALL SUBUNIT, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiPGTL_PELAC
AccessioniPrimary (citable) accession number: P80563
Secondary accession number(s): Q9S354
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 70 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3