PGTL_PELAC
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 03-AUG-2022, entry version 93.
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; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC 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}.
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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 PDBsum; 4V4C; -.
DR PDBsum; 4V4D; -.
DR PDBsum; 4V4E; -.
DR AlphaFoldDB; P80563; -.
DR SMR; P80563; -.
DR TCDB; 5.A.3.7.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR BRENDA; 1.97.1.2; 4585.
DR EvolutionaryTrace; P80563; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0018706; F:pyrogallol hydroxytransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
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 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 TURN 153..155
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 156..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 177..181
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 190..192
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:4V4E"
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 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 STRAND 646..648
FT /evidence="ECO:0007829|PDB:4V4D"
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 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
