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Database: UniProt
Entry: I4BXN5_ACEMN
LinkDB: I4BXN5_ACEMN
Original site: I4BXN5_ACEMN 
ID   I4BXN5_ACEMN            Unreviewed;       625 AA.
AC   I4BXN5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000256|PIRNR:PIRNR006439};
DE            Short=IOR {ECO:0000256|PIRNR:PIRNR006439};
DE            EC=1.2.7.8 {ECO:0000256|PIRNR:PIRNR006439};
DE   AltName: Full=Indolepyruvate ferredoxin oxidoreductase subunit alpha {ECO:0000256|PIRNR:PIRNR006439};
GN   OrderedLocusNames=Anamo_1440 {ECO:0000313|EMBL:AFM22042.1};
OS   Acetomicrobium mobile (strain ATCC BAA-54 / DSM 13181 / JCM 12221 / NGA)
OS   (Anaerobaculum mobile).
OC   Bacteria; Synergistota; Synergistia; Synergistales; Acetomicrobiaceae;
OC   Acetomicrobium.
OX   NCBI_TaxID=891968 {ECO:0000313|EMBL:AFM22042.1, ECO:0000313|Proteomes:UP000006061};
RN   [1] {ECO:0000313|Proteomes:UP000006061}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-54 / DSM 13181 / NGA
RC   {ECO:0000313|Proteomes:UP000006061};
RX   PubMed=23961311; DOI=10.4056/sigs.3547050;
RA   Mavromatis K., Stackebrandt E., Held B., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Mikhailova N., Huntemann M., Pati A.,
RA   Chen A., Palaniappan K., Land M., Rohde M., Spring S., Goker M., Woyke T.,
RA   Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of the moderate thermophile Anaerobaculum mobile
RT   type strain (NGA(T)).";
RL   Stand. Genomic Sci. 8:47-57(2013).
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative decarboxylation
CC       of arylpyruvates. {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|PIRNR:PIRNR006439};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006439};
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};
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DR   EMBL; CP003198; AFM22042.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4BXN5; -.
DR   STRING; 891968.Anamo_1440; -.
DR   KEGG; amo:Anamo_1440; -.
DR   PATRIC; fig|891968.3.peg.1431; -.
DR   eggNOG; COG4231; Bacteria.
DR   HOGENOM; CLU_017727_0_0_0; -.
DR   Proteomes; UP000006061; 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   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   PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR   PANTHER; PTHR43710:SF7; INDOLEPYRUVATE OXIDOREDUCTASE SUBUNIT IORA; 1.
DR   Pfam; PF00037; Fer4; 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   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR006439};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR006439};
KW   Iron {ECO:0000256|PIRNR:PIRNR006439};
KW   Iron-sulfur {ECO:0000256|PIRNR:PIRNR006439};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR006439};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006439};
KW   Pyruvate {ECO:0000313|EMBL:AFM22042.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006061};
KW   Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN          597..625
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   625 AA;  69321 MW;  2FE11651E208B103 CRC64;
     MALKDMGEML LREEPFSEIV MGDTAIVRAM VEAGVRVASS YPGSPTPEIA EAIASIPHER
     RPFYFEFSTN EKVALEVAFG ASINGHLSCC FFKSVGLNVA ADSFVQLSMM NLLGGMVMVL
     GDDPGANSSQ NEQDNRHLAR LAYVPVFEPA SPKESYEMFL EAAKLSKEHN MPVIVRLTTH
     VCHAKEKVRF GRWNPKPLDP TPRFDPKSGS YIPLTAATVY PMKRRALENV ERLREYAEFS
     PFNLFVKNDN NRRGIITAGL PFLSLMDVLQ FADEKPDILK LGMAYPLPRK LVADFLASHD
     EVKVLEELDN FIEVEVKSIA FDSGIKSRII GKKDLEDWVG EYVPEKVYSV MKKTWPDMLP
     DMDFSPKGPM PSPRPPQLCP GCGHRSAFYA IKRALKDTDI TVADIGCHTL GYLEPHEMGQ
     VMLCMGHSTG TGSGLSLFND ERKVVAFIGD STLFHAGLPG IINAVFNRHN MTLVIMENGT
     TAMTGHQDHP GSGKNFNGPT DAISIKKMLE GLGVKSIRVV DAYSQQKLTE AVREAVSEEG
     FSVVIASHPC MLKFTREQRR KGKLTKRQIS VDQEKCKRIY ECVKAFACPS FQLKDDGSVE
     VSEELCIGDG SCVQTCPVKA LRYED
//
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