IORA_METTM
ID IORA_METTM Reviewed; 618 AA.
AC P80910; D9PUX6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Indolepyruvate oxidoreductase subunit IorA;
DE Short=IOR;
DE EC=1.2.7.8;
DE AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha;
GN Name=iorA; OrderedLocusNames=MTBMA_c04220;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [2]
RP PROTEIN SEQUENCE OF 1-27, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=9108258; DOI=10.1111/j.1432-1033.1997.00862.x;
RA Tersteegen A., Linder D., Thauer R.K., Hedderich R.;
RT "Structures and functions of four anabolic 2-oxoacid oxidoreductases in
RT Methanobacterium thermoautotrophicum.";
RL Eur. J. Biochem. 244:862-868(1997).
CC -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC of arylpyruvates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] =
CC (indol-3-yl)acetyl-CoA + CO2 + H(+) + 2 reduced [2Fe-2S]-
CC [ferredoxin]; Xref=Rhea:RHEA:12645, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17640,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57271,
CC ChEBI:CHEBI:57287; EC=1.2.7.8;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:O07835};
CC Note=Binds 2 [4Fe-4S] clusters. In this family the first cluster has a
CC non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
CC {ECO:0000250|UniProtKB:O07835};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 10.0. {ECO:0000269|PubMed:9108258};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:9108258};
CC -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
CC {ECO:0000269|PubMed:9108258}.
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DR EMBL; CP001710; ADL58023.1; -; Genomic_DNA.
DR RefSeq; WP_013295249.1; NC_014408.1.
DR AlphaFoldDB; P80910; -.
DR STRING; 79929.MTBMA_c04220; -.
DR EnsemblBacteria; ADL58023; ADL58023; MTBMA_c04220.
DR GeneID; 9704128; -.
DR KEGG; mmg:MTBMA_c04220; -.
DR PATRIC; fig|79929.8.peg.411; -.
DR HOGENOM; CLU_017727_0_0_2; -.
DR OMA; IGDSTFM; -.
DR OrthoDB; 20764at2157; -.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR045025; HACL1-like.
DR InterPro; IPR017721; IorA.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR PANTHER; PTHR43710; PTHR43710; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR PIRSF; PIRSF006439; Indolepyruvate_ferr_oxidored; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR03336; IOR_alpha; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Repeat; Transport.
FT CHAIN 1..618
FT /note="Indolepyruvate oxidoreductase subunit IorA"
FT /id="PRO_0000099927"
FT DOMAIN 559..590
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 588..617
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 568
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 571
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 574
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 580
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 597
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 600
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 603
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT BINDING 607
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O07835"
FT CONFLICT 11
FT /note="R -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 67098 MW; E1D0F3A9B2B406AB CRC64;
MELDDILDAG RGDRLFLLGN EAAVRAAIES GVGVASTYPG TPSSEIGNVL SKIAKRAGIY
FEFSINEKVA LEVAAAAAAS GVRSFTFMKH VGLNVASDSF MSVAYTGVRA GMVVLSADDP
SMFSSQNEQD NRHYARLAWV PLLEPSNPQE ILEYMNHAFE LSEEYRIPVL LRTTTRVSHM
RGVVEAGERR AEPVKGFFRK NPEQFVPVPA TARVMRRELV EKMKKLKRVA DTSELNRVLN
EDSESDLGII ASGGAFNYVY DALQTLGLDV PVLKLGFTYP FPAGLVAEFL SGLEGVLVVE
EVDSVMEKEV LAVATSEGLD VGVHGKLDGT LPEIYEYSED IVRRAISGLT GIKSHEKGIE
APELPERPPA LCPGCPHRAM YYSVRRAASE LGIEGEDLIF PTDIGCYTLG IEPPYSAADY
LLSMGSSVGT ACGFSAATSQ RIVSFIGDST FFHAGIPPLI NAVHNRQRFV LVILDNRTTA
MTGGQPHPGL PVDGMGEEAP AISIEDITRA CGVEFVETVN PMNIRRSSET IRRALQHESV
AVVISRYPCM LSEGAVRGRP VRVDEEKCDL CLECLNELAC PAIVEEDGRV FIDPLYCRGC
TICLQICPAG AIKPEGKR
