ID H0E000_9ACTN Unreviewed; 712 AA.
AC H0E000;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 03-MAY-2023, entry version 31.
DE SubName: Full=Indolepyruvate oxidoreductase subunit IorA {ECO:0000313|EMBL:EHN12959.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:EHN12959.1};
GN ORFNames=PAI11_01050 {ECO:0000313|EMBL:EHN12959.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN12959.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN12959.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN12959.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(2013).
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:EHN12959.1}.
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; AGUD01000004; EHN12959.1; -; Genomic_DNA.
DR AlphaFoldDB; H0E000; -.
DR PATRIC; fig|1097667.3.peg.105; -.
DR Proteomes; UP000005143; Unassembled WGS sequence.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; 3.40.50.970; -; 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:SF5; INDOLEPYRUVATE FERREDOXIN OXIDOREDUCTASE ALPHA SUBUNIT; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR PIRSF; PIRSF006439; Indolepyruvate_ferr_oxidored; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:EHN12959.1};
KW Pyruvate {ECO:0000313|EMBL:EHN12959.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005143}.
FT DOMAIN 606..637
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 712 AA; 76396 MW; 7900E7B054B6A382 CRC64;
MQQLRHGAGT ELHVEGILAV TKALLQSGVA YVGGYQGAPI SHLMDVLGDA REILDELGVY
FENSASEATA AAMLAASVHY PLRGAVTFKS TVGLNVASDA LANLASGGVK GGALVILGED
YGEGSSIMQE RSHAFAMKSQ MWLLDPRPNI TAIVDAVEAG FELSEASNTP VMLDLRLRSC
HLHGAFTAKD NRRPPMTVKD AIENPARDVS RVVLPPASFQ HEQEKVNDRW PAAVRFIKER
GLNEVINDGA SDIGIITQGG LYNTLNRSME LLGCSDPFGN TQVPLYVMNV TYPVVDDEIV
AFCSGKRAVL LLEEGQPDYL EQNLNAILRR AGVDTALHGK DLLPVAGEYT SAAMTKGIAA
FLQRYQPDLV VHEPALLLDR DDPASPFASP VDPAAILPRP PGLCTGCPER PIFSGMKLAE
RETGQHHVSA DIGCHLFAIN APFDLGATTM GYGLGSAGAS ALNASGADRS TVAIMGDGGF
WHNGLTSGVG NAVFNKNDQV LVVVDNDYSA ATGGQDVLSS HADTPLRSTQ HPIEKAVRGI
GVEWAKTIDN TFDVTQVRDT FVEAFEAKDA GPKVLVMQSE CQLNRQRRVK PEMRKALKDG
KRVVRERFGV DAETCTGDHA CIRISGCPSL TIASNPDPMR TDPVAKVLDS CVGCGVCGNN
AHAAVLCPSF YRTDVVHNPT ARDKVLVRIR SWWMRALSRG LERRAARFEV AA
//