ID A0A1F8R5K7_9CHLR Unreviewed; 1107 AA.
AC A0A1F8R5K7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000256|ARBA:ARBA00017710};
DE EC=1.2.7.8 {ECO:0000256|ARBA:ARBA00012812};
DE AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000256|ARBA:ARBA00030514};
GN ORFNames=A2Z05_02270 {ECO:0000313|EMBL:OGO42958.1};
OS Chloroflexi bacterium RBG_16_60_22.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797656 {ECO:0000313|EMBL:OGO42958.1, ECO:0000313|Proteomes:UP000179512};
RN [1] {ECO:0000313|EMBL:OGO42958.1, ECO:0000313|Proteomes:UP000179512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC of arylpyruvates. {ECO:0000256|ARBA:ARBA00002995}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBUNIT: Heterodimer of the IorA and IorB subunits.
CC {ECO:0000256|ARBA:ARBA00011238}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGO42958.1}.
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; MGNX01000108; OGO42958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8R5K7; -.
DR STRING; 1797656.A2Z05_02270; -.
DR Proteomes; UP000179512; Unassembled WGS sequence.
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 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; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
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; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF01855; POR_N; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 2.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 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; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:OGO42958.1};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1070..1099
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1107 AA; 119104 MW; 509B53F332BC7C13 CRC64;
MSKVAEITIT SDAPGARLFM LGNEAIARGA IEAGVQVVAS YPGTPSSEIT EALVGMADRM
GFYAEWSVNE KVAMEVAMAA SISGLKSLAI MKHVGVNVAH DPLMSASYMG ARGGLVLISA
DDPGQWSSQN EQDNRYIARQ AYIPVLEPSS AQEAKDMMAN AFRLSEEFNQ MFMLRSVTRL
GHGRSDIVFG EIEREKRAGK FVKDPGRLVC LPANFRNNRR LVVARMEKIR QAVDAWPYNR
LTLKKNAKLG IIATGIAYGY AIEAVQWLGL EDKVSVLKVG TPYPLPAELT KQMLKAVPEV
LVVEELEPFV EEAVKVVAKD AGLTTKVHGK DMLSVVGELS TRQVSEALSK LTGALPPVDF
AMLDRIKAET QSLLPLRPPT MCAGCPHRAT AYAINIACRR YQQETGREPV KTGDIGCYAL
AANPPLNSDD VAVCMGGAFG LANGFAHVVD APVVAHLGDS TFFHSGIPPM INAVYNKSRV
TMVVMDNATT GMTGFQPHPG ASGDVSVDIK IEDIARASGV KFVEVVDSFD LPKLIETLDK
ALRFDGPSVI VARRLCGILD QREKRKQGVK TVPWEVEEEK CLAGAPPYCQ ATCPLHIDIR
GYTRLIKEGK FNEALAIIKQ TLPFPAIIGR ICTRPCEARC QRAEVEEAIA INALKRAASD
FGKYKEGYSV KAEKKEKVAI VGGGPAGIMA AYDLRKAGYK VTIFEALPRL GGMMAVGIPE
FRLPRDILDK ETAIIKKLGV EIKLNTRVGK DVKMSDLKKD YHAVFIAVGA HRGRNLGIEN
EKAPGVIDGT EFLLKVNTGQ KVAVPDRVAV VGGGNVAIDC ARTGVRLGCP DVTIVYRRSR
AEMPAIAEEI AGAESEGVKI RLLAGPNKVV LKGNKVSGLE CIKMKLGEPD KSGRRRPVPV
AGSEFTVAAD LIIAAVGEEP DLALMTGDMT KAVKDGLVKA DPLTLETGIP GVFAGGDAVT
GPATVIQAMA AGRKAAVSID RFLKGEQLDT GREGEAVFES KLIVDTFGIT PESRLDMPLL
PVAQRRGNFR EVELGLSQEE AVREAKRCLS CDCHICIDLT GCPALITEDD RVKIDQESCP
GCGVCAQVCP HDAIFLPGAK DGRDERA
//