ID A0A080M8V7_9PROT Unreviewed; 1176 AA.
AC A0A080M8V7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:KFB77717.1};
GN ORFNames=AW06_001091 {ECO:0000313|EMBL:KFB77717.1};
OS Candidatus Accumulibacter cognatus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX NCBI_TaxID=2954383 {ECO:0000313|EMBL:KFB77717.1, ECO:0000313|Proteomes:UP000021315};
RN [1] {ECO:0000313|EMBL:KFB77717.1, ECO:0000313|Proteomes:UP000021315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-02 {ECO:0000313|Proteomes:UP000021315};
RA Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT clades.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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:KFB77717.1}.
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DR EMBL; JDST02000018; KFB77717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A080M8V7; -.
DR STRING; 1453999.AW06_001091; -.
DR Proteomes; UP000021315; Unassembled WGS sequence.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; 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; IPR009014; Transketo_C/PFOR_II.
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 SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:KFB77717.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000021315}.
FT DOMAIN 653..683
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1176 AA; 128810 MW; 82A0FBF6B4EBF485 CRC64;
MGDLSTTLDS RYTANSGRVF LSGTQALVRL PMLQRMRDEA AGLNTAGFVS GYRGSPLGGL
DQALWKARPH LDARRIVFQP GVNEDLAATA VWGTQQLNLF PGAKYEGVFA MWYGKGPGVD
RCGDVFRHAN AAGSAKHGGV LVIAGDDHAA KSSTLPHQTE HVFKAVMMPV LYPANVQEYL
DYGLHGWAMS RYSGCWVVMK ALADTVETSA SVSIDPLSIQ IRLPDDFEMP KNDPHALNIR
WPDPPLQQEA RLLNHKLYAA LAYCRANQLN RVVIDSADPA SPARLGIITA GKAYLDVRQA
LDELGIDDEL AAQIGIRLYK VGMVWPLEAD GVRRFAEGLE EILVVEEKRQ LLEYQLKEEL
YNWREDVRPR VVGKFDEKGE WALLPTGSGH LTHGDWLLPA AGELSVAQVA RALAARIGRF
FTSSAIEARL ALLEAKQRSL AQGLLPATGM AAIQRTPYFC SGCPHNTSTR VPEGSRAVAG
IGCHYMVTWM DRNTATFTHM GGEGVTWVGQ APFSSEKHIF ANLGDGTYFH SGLLAIRQAV
AAGVAITYKI LYNDAVAMTG GQPVDGPLSV AQLSRQLAAE GIQRIVIVTD EPEKYRKVPD
LAPNTPIHHR DQLDAVQREL RNHPGVSVLI YDQTCATEKR RRRKRGKLAD PARRVFINTA
VCEGCGDCGV QSNCLAVIPV ETEFGRKRAI DQSACNKDFS CIQGFCPSFV SVEGGRLRRG
RAIAAAEAVL PEPLLPDTRH PYNILITGVG GTGVVTLGAL LGMAAHLDGK GVSVLDMTGL
AQKFGTVFSH LRIADRPEDI HAARIATGEA HAVIGGDLVV SAGAEALSKV LAGKTRAVVN
VAETPTAEFT RNPDWQFPQE HLQEQISEAC GEGNALFLDT AAMSRRLMGD ALYGNLLLLG
VAWQRGLVPL SLAAIDQAIE LNATAVEQNR QAFLWGRRAA HDPEALQNLL NPTGMPAPQR
LSRNLDELIR QRVETLTAYQ NARYAERYRA LVERVSAAES PLQSTALSEA VARSYFRLLA
VKDEYEVARL HSDPAFLQQL SEEFEGDYRL RFHLAPPLLA RLDPATGRVR KSSYGPWMMS
IFKGLSRLRF LRGTIFDPFG KTQERRMERQ LLADYEADVE LMLTRLEEKT QAIAIELAKV
PEQIRGYGHV KAASVLPARA RRAMLRAQLE ALANAS
//