ID PGTL_PELAC Reviewed; 875 AA. AC P80563; Q9S354; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 103. DE RecName: Full=Pyrogallol hydroxytransferase large subunit; DE EC=1.97.1.2; DE AltName: Full=Transhydroxylase subunit alpha; GN Name=athL; OS Pelobacter acidigallici. OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfuromonadia; OC Desulfuromonadales; Desulfuromonadaceae; Pelobacter. OX NCBI_TaxID=35816; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Retey J.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP PROTEIN SEQUENCE OF 2-17. RC STRAIN=ATCC 49970 / DSM 2377 / Ma Gal2 / Braunschweig; RX PubMed=8647079; DOI=10.1111/j.1432-1033.1996.0406k.x; RA Reichenbecher W., Ruediger A., Kroneck P.M.H., Schink B.; RT "One molecule of molybdopterin guanine dinucleotide is associated with each RT subunit of the heterodimeric Mo-Fe-S protein transhydroxylase of Pelobacter RT acidigallici as determined by SDS/PAGE and mass spectrometry."; RL Eur. J. Biochem. 237:406-413(1996). RN [3] RP CHARACTERIZATION. RX PubMed=10082952; DOI=10.1016/s0167-4838(99)00004-7; RA Reichenbecher W., Schink B.; RT "Towards the reaction mechanism of pyrogallol-phloroglucinol RT transhydroxylase of Pelobacter acidigallici."; RL Biochim. Biophys. Acta 1430:245-253(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-874 IN COMPLEXES WITH RP MO-BIS-MGD; SUBSTRATE OR INHIBITOR AND THE SMALL SUBUNIT, COFACTOR, AND RP SUBUNIT. RX PubMed=15284442; DOI=10.1073/pnas.0404378101; RA Messerschmidt A., Niessen H., Abt D., Einsle O., Schink B., Kroneck P.M.; RT "Crystal structure of pyrogallol-phloroglucinol transhydroxylase, an Mo RT enzyme capable of intermolecular hydroxyl transfer between phenols."; RL Proc. Natl. Acad. Sci. U.S.A. 101:11571-11576(2004). CC -!- FUNCTION: Isomerization of pyrogallol to phloroglucin. CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = CC 1,2,3,5-tetrahydroxybenzene + 1,3,5-trihydroxybenzene; CC Xref=Rhea:RHEA:21000, ChEBI:CHEBI:16164, ChEBI:CHEBI:16204, CC ChEBI:CHEBI:16746; EC=1.97.1.2; CC -!- COFACTOR: CC Name=Mo-bis(molybdopterin guanine dinucleotide); CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000269|PubMed:15284442}; CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo- CC bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:15284442}; CC -!- SUBUNIT: Heterodimer of a large and a small subunit. CC {ECO:0000269|PubMed:15284442}. CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ243850; CAB50913.1; -; Genomic_DNA. DR PIR; S65430; S65430. DR PDB; 4V4C; X-ray; 2.35 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-875. DR PDB; 4V4D; X-ray; 2.20 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-875. DR PDB; 4V4E; X-ray; 2.00 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-875. DR AlphaFoldDB; P80563; -. DR SMR; P80563; -. DR TCDB; 5.A.3.7.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family. DR KEGG; ag:CAB50913; -. DR BRENDA; 5.4.4.9; 4585. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter. DR GO; GO:0009055; F:electron transfer activity; IEA:TreeGrafter. DR GO; GO:0030151; F:molybdenum ion binding; IEA:TreeGrafter. DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro. DR GO; GO:0018706; F:pyrogallol hydroxytransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009061; P:anaerobic respiration; IEA:TreeGrafter. DR CDD; cd02777; MopB_CT_DMSOR-like; 1. DR CDD; cd02751; MopB_DMSOR-like; 1. DR Gene3D; 2.20.25.340; -; 1. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 3.40.50.740; -; 2. DR InterPro; IPR049032; AhtL-like_N. DR InterPro; IPR009010; Asp_de-COase-like_dom_sf. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR050612; Prok_Mopterin_Oxidored. DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1. DR PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1. DR Pfam; PF21423; AhtL-like_1st; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR SUPFAM; SSF50692; ADC-like; 1. DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1. DR PDBsum; 4V4C; -. DR PDBsum; 4V4D; -. DR PDBsum; 4V4E; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Metal-binding; Molybdenum; KW Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:8647079" FT CHAIN 2..875 FT /note="Pyrogallol hydroxytransferase large subunit" FT /id="PRO_0000063242" FT REGION 82..104 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 175 FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)" FT /ligand_id="ChEBI:CHEBI:60539" FT /ligand_part="Mo" FT /ligand_part_id="ChEBI:CHEBI:28685" FT STRAND 5..9 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 16..21 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 24..29 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 39..42 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 44..46 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 49..51 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 61..64 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 67..70 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:4V4C" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 93..95 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 98..101 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 105..108 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 114..131 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 134..136 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 137..140 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 149..151 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 153..157 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 158..164 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 167..170 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 179..183 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 184..187 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 201..208 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 210..216 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 219..222 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 228..231 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 232..240 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 254..259 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 271..284 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 290..296 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 300..307 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 308..312 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 318..325 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 329..341 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 344..348 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 349..352 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 356..358 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 363..376 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 377..380 FT /evidence="ECO:0007829|PDB:4V4C" FT STRAND 389..391 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 404..406 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:4V4C" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 417..419 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 422..426 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 429..431 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 438..441 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 446..448 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 449..451 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 452..458 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 461..464 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 475..477 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 479..483 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 487..490 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 492..497 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 500..503 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 504..506 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 508..513 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 521..529 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 533..535 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 537..542 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 545..547 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 550..553 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 564..567 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 568..570 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 572..576 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 589..599 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 603..607 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 612..621 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 625..627 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 631..637 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 639..641 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 642..644 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 655..658 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 672..674 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 686..691 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 693..700 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 715..717 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 721..723 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 725..728 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 732..735 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 746..749 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 753..756 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 758..760 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 761..764 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 767..775 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 776..781 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 789..794 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 797..809 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 813..815 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 825..828 FT /evidence="ECO:0007829|PDB:4V4E" FT TURN 829..831 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 834..836 FT /evidence="ECO:0007829|PDB:4V4E" FT HELIX 839..841 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 848..851 FT /evidence="ECO:0007829|PDB:4V4E" FT STRAND 860..866 FT /evidence="ECO:0007829|PDB:4V4E" SQ SEQUENCE 875 AA; 99261 MW; B5D7DE5FAEF53A61 CRC64; MGEVVRLTNS STGGPVFVYV KDGKIIRMTP MDFDDAVDAP SWKIEARGKT FTPPRKTSIA PYTAGFKSMI YSDLRIPYPM KRKSFDPNGE RNPQLRGAGL SKQDPWSDYE RISWDEATDI VVAEINRIKH AYGPSAILST PSSHHMWGNV GYRHSTYFRF MNMMGFTYAD HNPDSWEGWH WGGMHMWGFS WRLGNPEQYD LLEDGLKHAE MIVFWSSDPE TNSGIYAGFE SNIRRQWLKD LGVDFVFIDP HMNHTARLVA DKWFSPKIGT DHALSFAIAY TWLKEDSYDK EYVAANAHGF EEWADYVLGK TDGTPKTCEW AEEESGVPAC EIRALARQWA KKNTYLAAGG LGGWGGACRA SHGIEWARGM IALATMQGMG KPGSNMWSTT QGVPLDYEFY FPGYAEGGIS GDCENSAAGF KFAWRMFDGK TTFPSPSNLN TSAGQHIPRL KIPECIMGGK FQWSGKGFAG GDISHQLHQY EYPAPGYSKI KMFWKYGGPH LGTMTATNRY AKMYTHDSLE FVVSQSIWFE GEVPFADIIL PACTNFERWD ISEFANCSGY IPDNYQLCNH RVISLQAKCI EPVGESMSDY EIYRLFAKKL NIEEMFSEGK DELAWCEQYF NATDMPKYMT WDEFFKKGYF VVPDNPNRKK TVALRWFAEG REKDTPDWGP RLNNQVCRKG LQTTTGKVEF IATSLKNFEE QGYIDEHRPS MHTYVPAWES QKHSPLAVKY PLGMLSPHPR FSMHTMGDGK NSYMNYIKDH RVEVDGYKYW IMRVNSIDAE ARGIKNGDLI RAYNDRGSVI LAAQVTECLQ PGTVHSYESC AVYDPLGTAG KSADRGGCIN ILTPDRYISK YACGMANNTA LVEIEKWDGD KYEIY //