ID A0A0S1Y4T7_9BORD Unreviewed; 1225 AA.
AC A0A0S1Y4T7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:ALM85026.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:ALM85026.1};
GN ORFNames=ASB57_20435 {ECO:0000313|EMBL:ALM85026.1};
OS Bordetella sp. N.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM85026.1, ECO:0000313|Proteomes:UP000064621};
RN [1] {ECO:0000313|EMBL:ALM85026.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N {ECO:0000313|EMBL:ALM85026.1};
RA Hou L.;
RT "Draft genome of Bordetella sp. N.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013111; ALM85026.1; -; Genomic_DNA.
DR RefSeq; WP_057653878.1; NZ_CP013111.1.
DR AlphaFoldDB; A0A0S1Y4T7; -.
DR STRING; 1746199.ASB57_20435; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000064621; Chromosome.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
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; -; 1.
DR Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR046667; DUF6537.
DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat.
DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N.
DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR48084:SF4; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB; 1.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR Pfam; PF20169; DUF6537; 1.
DR Pfam; PF01558; POR; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ALM85026.1}; Pyruvate {ECO:0000313|EMBL:ALM85026.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000064621}.
FT DOMAIN 652..684
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1225 AA; 132785 MW; 1AAF7A3013FFDED5 CRC64;
MNAPLTPAQR AALASVQLDD KYTLHTGRAW MSGIHALVRL PMLQRVRDLA AGLNTAGFVS
GYRGSPLGGV DLNMWKAAKY LKEHHVEFQP GINEDLAATA VWGSQQVNLF PGARYDGVFG
MWYGKGPGVD RSGDVFKHAN AAGTSKHGGV LVVAGDDHPA KSSTLPHQSD HIFKACLIPV
LFPSSVQEVL DFGLHGWAMS RYAGVWVGMK CITDIVEVSA SVDVAADRVR ILLPEDFHMP
PDGLNIRLPD TPLQQEARLL DYKLYAALSY ARANGLNREL WQVPADQARF GIMTSGKAYL
DTRQALADLG LTDDVCGRIG VRLFKVGMVW PLEATGTQRF AEGLDEILVV EEKRQVLEYQ
LKEELFGWIG TGRKIPRVVG KFDDKDGGEW SVPQGNWLLP AHYEFSPAIV AKVIGARLLR
FELPDDVRAG IQARLAVIEA AERALARPRV VADRKPWFCS GCPHNTSTRV PDGSRGMAGI
GCHYMVTWMG RNTQVFTQMG GEGVPWIGQA PFTDEKHVFA NLGDGTYYHS GLLAIRAAVA
AKVPITYKIL FNDAVAMTGG QPVDGPINVP MITQQMAAEG IEKIVVVTDE PEKYRNVQGL
APGVPVHHRD ELDEVMRELR EYPNVSVLVY DQTCATEKRR RRKHNAYPDP ARRVVINERV
CEGCGDCSDK SHCLSVEPLE TEFGRKRVIN QSSCNKDFSC LKGFCPSFVT VEGGKLRQPK
ALAQDGAVDA GVPAPALPEL RAAYGIFIAG VGGTGVVTIG QLLGMAAHIE GKGCSVLDMA
GLAQKGGAVH SHVVLAASPA DLLNTRVAMG EADVVLAGDL VVATGQDALA RMRVDRTRLL
LNSDVAPTAA FVNNPDWHLP GSDLLQDLRR ACGAGNVHAM DAAELAVGLL GDAIYANPLM
LGYAWQKGWI PLSDESLLRA IELNGQQIPK NQAAFAWGRR AAQDLAAVQA LIQAPAGGAG
TRLDADGAEV IEIRRGARSA APANTDAATG SAGMAPATSA RRLPAAVQAL VGTRSDFLAQ
YQNAAYARGY EELVEQVAVA EQAATGTSRL AEAVARYYFK LLAYKDEYEV ARLYTDGEFL
AAVNRQFEGD WKLSFHLAPP TFSRRDKQGH LIKRAYGPWM LKAFGVLARL RFLRGTPLDP
FGRTAERRAE RALIEEYRNT LTRAILPKLD RGNLDAAVAL ASLPEQIRGY GHVKDAAMEK
AAKQRTALLE KFTAPVREIG GARAA
//
