ID A5UK69_METS3 Unreviewed; 632 AA.
AC A5UK69;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000256|ARBA:ARBA00017710, ECO:0000256|PIRNR:PIRNR006439};
DE Short=IOR {ECO:0000256|PIRNR:PIRNR006439};
DE EC=1.2.7.8 {ECO:0000256|ARBA:ARBA00012812, ECO:0000256|PIRNR:PIRNR006439};
DE AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000256|ARBA:ARBA00030514, ECO:0000256|PIRNR:PIRNR006439};
GN OrderedLocusNames=Msm_0392 {ECO:0000313|EMBL:ABQ86597.1};
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247 {ECO:0000313|EMBL:ABQ86597.1, ECO:0000313|Proteomes:UP000001992};
RN [1] {ECO:0000313|EMBL:ABQ86597.1, ECO:0000313|Proteomes:UP000001992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS
RC {ECO:0000313|Proteomes:UP000001992};
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC of arylpyruvates. {ECO:0000256|ARBA:ARBA00002995,
CC ECO:0000256|PIRNR:PIRNR006439}.
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 Evidence={ECO:0000256|ARBA:ARBA00033657,
CC ECO:0000256|PIRNR:PIRNR006439};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|PIRNR:PIRNR006439,
CC ECO:0000256|PIRSR:PIRSR006439-50};
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:0000256|PIRNR:PIRNR006439, ECO:0000256|PIRSR:PIRSR006439-50};
CC -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
CC {ECO:0000256|ARBA:ARBA00011238, ECO:0000256|PIRNR:PIRNR006439}.
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DR EMBL; CP000678; ABQ86597.1; -; Genomic_DNA.
DR RefSeq; WP_004032135.1; NZ_CP117965.1.
DR AlphaFoldDB; A5UK69; -.
DR STRING; 420247.Msm_0392; -.
DR EnsemblBacteria; ABQ86597; ABQ86597; Msm_0392.
DR GeneID; 78817020; -.
DR KEGG; msi:Msm_0392; -.
DR PATRIC; fig|420247.28.peg.395; -.
DR eggNOG; arCOG01609; Archaea.
DR HOGENOM; CLU_017727_0_0_2; -.
DR BioCyc; MSMI420247:GHWZ-397-MONOMER; -.
DR Proteomes; UP000001992; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; cd02008; TPP_IOR_alpha; 1.
DR CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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_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; PF12837; Fer4_6; 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; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRNR:PIRNR006439};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR006439};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR006439};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR006439};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006439};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR006439}; Pyruvate {ECO:0000313|EMBL:ABQ86597.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006439}.
FT DOMAIN 571..595
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 602..631
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 582
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 585
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 588
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 594
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 611
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 614
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 617
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
FT BINDING 621
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006439-50"
SQ SEQUENCE 632 AA; 68791 MW; F9F9031AE734479D CRC64;
MNLKELVTGK PGDKQFLLGN EAAVRGVIEA GVSVAATYPG TPSSEIGNVL SGLAKEANIY
FEFSTNEKVA MEVAATAAAS GLRSFTFMKH VGMNVASDSF MTTAYSGVNG GMVILSADDP
SLFSSQNEQD TRNYGRLANV PILEPSNCQE VKDMVKYAFD LSEQFKLPVI VRTTTRVSHM
RGVVEFGEVV DNSSEGESHW KKGFFKKNPA QFVPVPAFAK DMHVALVEKM DEINKITNES
DFNVESYFSQ NKKYGVIASS SAYNYAYDVI RYNNLDIDVL KLGFSYPFPY DKVADFVKDY
DEVFIVEEVD PIIEKDTLVA IGKNNLNTVV HGKLDGTFPV YHEFNSDIVA NGFNKYLNFI
EENTDDYSDN LLNLQEEIPS RAPVLCAGCP HRAMYYGVNK ALEELGIPLK DAVFASDIGC
YTLGINPPYN AADYLLSMGS SVGDGCGFSI ATNQKVISFI GDSTFFHSGI SPLINAVHNK
NNFILTVLDN RITAMTGGQP NPGIPVDGMG DDAPEISIRK LALACGCNYV RVINPLNLDQ
VVKTYKEALE RDEVCVIIAK APCTLIKGKT RKPPVNYIDS NCNGCNKCVS ELACPAISKD
GGKIAIDQSM CDGCGVCIQV CKYGALEAGR GE
//
