PGTS_PELAC
ID PGTS_PELAC Reviewed; 274 AA.
AC P80564; Q9XAY5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Pyrogallol hydroxytransferase small subunit;
DE EC=1.97.1.2;
DE AltName: Full=Transhydroxylase subunit beta;
GN Name=bthL;
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 1-15.
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).
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 3 [4Fe-4S] clusters.;
CC -!- SUBUNIT: Heterodimer of a large and a small subunit.
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DR EMBL; AJ243850; CAB50914.1; -; Genomic_DNA.
DR PIR; S65429; S65429.
DR PDB; 4V4C; X-ray; 2.35 A; B/D/F/H/J/L/N/P/R/T/V/X=1-274.
DR PDB; 4V4D; X-ray; 2.20 A; B/D/F/H/J/L/N/P/R/T/V/X=1-274.
DR PDB; 4V4E; X-ray; 2.00 A; B/D/F/H/J/L/N/P/R/T/V/X=1-274.
DR PDBsum; 4V4C; -.
DR PDBsum; 4V4D; -.
DR PDBsum; 4V4E; -.
DR AlphaFoldDB; P80564; -.
DR SMR; P80564; -.
DR TCDB; 5.A.3.7.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR BRENDA; 1.97.1.2; 4585.
DR EvolutionaryTrace; P80564; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0018706; F:pyrogallol hydroxytransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF13247; Fer4_11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase.
FT CHAIN 1..274
FT /note="Pyrogallol hydroxytransferase small subunit"
FT /id="PRO_0000058366"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:4V4E"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:4V4E"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4V4E"
FT TURN 96..101
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:4V4E"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 161..171
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:4V4E"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 197..205
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 254..265
FT /evidence="ECO:0007829|PDB:4V4E"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:4V4E"
SQ SEQUENCE 274 AA; 31221 MW; 2F9A9CD24082F5A1 CRC64;
MEQYYMVIDV AKCQDCNNCF MGCMDEHELN EWPGYTASMQ RGHRWMNIER RERGTYPRND
INYRPTPCMH CENAPCVAKG NGAVYQREDG IVLIDPEKAK GKKELLDTCP YGVMYWNEEE
NVAQKCTMCA HLLDDESWAP KMPRCAHNCG SFVYEFLKTT PEAMAKKVEE EGLEVIKPEL
GTKPRVYYKN LYRFEKNYVT AGILVQGDCF EGAKVVLKSG GKEVASAETN FFGEFKFDAL
DNGEYTVEID ADGKSYSDTV VIDDKSVDLG FIKL
