(data stored in ACNUC7421 zone)

SWISSPROT: Q2ILY7_ANADE

ID   Q2ILY7_ANADE            Unreviewed;       546 AA.
AC   Q2ILY7;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 75.
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=Adeh_0040 {ECO:0000313|EMBL:ABC79818.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC79818.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ferredoxin-dependent oxidative
CC       decarboxylation of arylpyruvates. {ECO:0000256|PIRNR:PIRNR006439}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + indole-3-pyruvate + 2 oxidized [2Fe-2S]-
CC         [ferredoxin] = CO2 + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] + S-
CC         2-(indol-3-yl)acetyl-CoA; Xref=Rhea:RHEA:12645, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:17640, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57271, ChEBI:CHEBI:57287;
CC         EC=1.2.7.8; 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
CC       has a non-standard and varying [4Fe-4S] binding motif
CC       CX(2)CX(2)CX(4-5)CP. {ECO:0000256|PIRNR:PIRNR006439};
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DR   EMBL; CP000251; ABC79818.1; -; Genomic_DNA.
DR   RefSeq; WP_011419101.1; NC_007760.1.
DR   STRING; 290397.Adeh_0040; -.
DR   EnsemblBacteria; ABC79818; ABC79818; Adeh_0040.
DR   KEGG; ade:Adeh_0040; -.
DR   eggNOG; ENOG4105BZI; Bacteria.
DR   eggNOG; COG4231; LUCA.
DR   HOGENOM; HOG000224871; -.
DR   KO; K00179; -.
DR   OMA; TFLHTGI; -.
DR   BioCyc; ADEH290397:G1G5W-42-MONOMER; -.
DR   Proteomes; UP000001935; 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   InterPro; IPR017721; Indolepyruvate_Fd_OxRdtase_asu.
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   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.
PE   4: Predicted;
DR   PRODOM; Q2ILY7.
DR   SWISS-2DPAGE; Q2ILY7.
KW   4Fe-4S {ECO:0000256|PIRNR:PIRNR006439};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
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|PIRNR:PIRNR006439};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006439};
KW   Pyruvate {ECO:0000313|EMBL:ABC79818.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Transport {ECO:0000256|PIRNR:PIRNR006439}.
FT   DOMAIN       15    165       POR_N. {ECO:0000259|Pfam:PF01855}.
FT   DOMAIN      358    506       TPP_enzyme_C. {ECO:0000259|Pfam:PF02775}.
SQ   SEQUENCE   546 AA;  57713 MW;  68B85213A33E580A CRC64;
     MERRLLSGDE AVAAAARDAG VRLGTGYPGT PSTEILQALD ALGGRAQWAP NEKVALEVGL
     GAAFGGARAL VTMKHVGLNV AADPLFTAAY TGVKGGLVVV SADDPGMASS QNEQDNRHYA
     VAAGLPMLEP ADSQEAYDLT VAAFELSERF AIPVILRMTT RVCHSKTLAA RRADLPAPPA
     PAFVRDIPGR VMIPAYARPA HRRLRKKLEA LQAFAEETPL NVWVKGDRAL GVITSGVTAR
     HVAEAAPSAS RLELKTVYPL PLEKIRAFAA SVDRCVVVEE GDPVFADAIR AAGIAVESKE
     APYRFGELDV QRVRRILARD PSPEPELPKG RPPALCEACP YHPVYATLRK LDCIVAGDIG
     CYTLGVLPPY QGIDTCVAMG ASLGVGLGLR HVLPEADARR VVSIIGDSTF IHTGLNGLVE
     MVYNPPPTGH VLVVLDNGTT AMTGQQEHPG TGRTLDHEPT GKVSIEGLAR ALGVANVDVI
     DPVADPAGWE ELLKERLAEP KLSVIIARRP CILAAADIRR YEKAADEKRA ALACAGCAGA
     GEVSDA
//

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