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 04-NOV-2026, entry version 103. 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; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanobacteria; Methanobacteriales; Methanobacteriaceae; OC 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=indole-3-pyruvate + 2 oxidized [2Fe-2S]-[ferredoxin] + CoA = CC (indol-3-yl)acetyl-CoA + 2 reduced [2Fe-2S]-[ferredoxin] + CO2 + CC H(+); 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}. 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; CP001710; ADL58023.1; -; Genomic_DNA. DR RefSeq; WP_013295249.1; NC_014408.1. DR AlphaFoldDB; P80910; -. DR STRING; 79929.MTBMA_c04220; -. DR PaxDb; 79929-MTBMA_c04220; -. DR GeneID; 77399201; -. DR GeneID; 9704128; -. DR KEGG; mmg:MTBMA_c04220; -. DR PATRIC; fig|79929.8.peg.411; -. DR HOGENOM; CLU_017727_0_0_2; -. DR OMA; AACAMKH; -. DR OrthoDB; 19071at2157; -. DR Proteomes; UP000000345; Chromosome. DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProtKB-ARBA. DR CDD; cd02008; TPP_IOR_alpha; 1. DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1. DR FunFam; 3.40.50.970:FF:000039; Indolepyruvate oxidoreductase subunit IorA; 1. DR Gene3D; 3.30.70.20; -; 1. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR045025; HACL1-like. DR InterPro; IPR063976; IOR_mid. DR InterPro; IPR017721; IorA. DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR011766; TPP_enzyme_TPP-bd. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR NCBIfam; TIGR03336; IOR_alpha; 1. DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1. DR PANTHER; PTHR43710:SF7; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORA; 1. DR Pfam; PF31012; IOR_mid; 1. DR Pfam; PF01855; POR_N; 1. DR Pfam; PF02775; TPP_enzyme_C; 1. DR PIRSF; PIRSF006439; Indolepyruvate_ferr_oxidored; 1. DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. DR SUPFAM; SSF52922; TK C-terminal domain-like; 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; Reference proteome; 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 //