ID N9W964_9SPHN Unreviewed; 1168 AA.
AC N9W964;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:ENY80193.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:ENY80193.1};
GN ORFNames=EBMC1_15569 {ECO:0000313|EMBL:ENY80193.1};
OS Sphingopyxis sp. MC1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1174684 {ECO:0000313|EMBL:ENY80193.1, ECO:0000313|Proteomes:UP000013072};
RN [1] {ECO:0000313|EMBL:ENY80193.1, ECO:0000313|Proteomes:UP000013072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC1 {ECO:0000313|EMBL:ENY80193.1,
RC ECO:0000313|Proteomes:UP000013072};
RA Lolas I.B., Kjeldal H., Almeida B., Le-Quy V., Gough H.L., Nielsen J.L.;
RT "Differential expression analysis of membrane associated proteins from
RT triclosan-degrading sphingopyxis.";
RL Submitted (FEB-2013) 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:ENY80193.1}.
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DR EMBL; AOUN01000017; ENY80193.1; -; Genomic_DNA.
DR RefSeq; WP_003050635.1; NZ_AOUN01000017.1.
DR AlphaFoldDB; N9W964; -.
DR PATRIC; fig|1174684.3.peg.3142; -.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG4231; Bacteria.
DR Proteomes; UP000013072; Unassembled WGS sequence.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
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; 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 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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ENY80193.1}; Pyruvate {ECO:0000313|EMBL:ENY80193.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000013072}.
FT DOMAIN 731..917
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 945..1143
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1168 AA; 125753 MW; DABA999E194A8737 CRC64;
MTQIATKARS PKVSLDDKWT RESGRVVMNG SQAIVRTMLE QKRRDSAAGL NTAGYVTGYR
GSPLGNVDTA MWSAGKYLQA ADVLFRPGVN EDLAATAVRG TQQLDAVEGA RFDGVFAAWY
GKGPGVDRSG DAFKHGNYAG THRNGGVIAY FGDDHVGKSS TVSHQSEQAM AASSIPCLYP
ANVEELLDHG LMAIAMSRYC GLWVGVKCVT EVAEQTANVD LDMLTRQYVL PETDDATNVH
MSAGTFNPLG EERVVVEHRL PRAQAFVRAN RIDRTIFDPV ADGIGIVASG KSYGDTRSAL
ELLGIDEARA RALGVSLYKV GCIWPLEPAG LTEFAERQAV LLFIEEKKAF LEAQAAAHLI
NMPGRPLFVG KQDEDGQALF STVDALEPVD IAKIIVGRLD RLGRADRALH EAAEQMPASQ
SVAGSGPAGP KRAPYFCSGC PHNRSTKVPE GSTSMTGIGC HTMVNFVRPD IALLPTQMGA
EGTNWVGLAP FVDTPHMFQN LGDGTYFHSG LMAIRAAVAA GTNITYKILY NDAVAMTGGQ
PVDGSISVAE IARQVQAEGV VEVIVLSDDP DRHRNTGLPA NVRVGHRDEL DAVQRHLREV
KGTTVLIYEQ TCAAEKRRRR KRGQFPDPAK RLFIAKEVCE GCGDCSVQST CVSLTPVETA
MGRKREIDQS SCNKDYSCLN GFCPSFITVR GAEPRKPSAL EIDEARFAAI PTPPVAPLDQ
DGFDIIVAGI GGTGVVTVGA LIGMAAHMEG KRMSLFDMTG LSQKNGAVYS HVRISDGARR
PATQRIARGG ADLLLAFDMV AGTGAEAVDT LRMGKTRAIA NTDLTATVAF QFDRSAQLDR
FMLLSKFEKL VGKDAICSVD ASSLARKVLG DTIGANMFMV GIAAQMGLLP VGVEALESAI
ELNGVSVGFN RKALHLGRLY VSDPAFLESL TRSDTDRPEV LPTGLDEIVA HRSAHLEQYQ
NAALASSYRA LVSKVADAER AVAPQSEDLA VAVALNYAKL LAYKDEYEVA RLLTSPKLRE
ELDRTFADGG RISFNMAPPI LNGGEIDGRP RKREFGPWIL PVLRVMARMK RLRGSVLDPF
ARNSERKRER ALIAEYEALV EETVARLTAT NLPVAVKLLS LADMIRGFGP VKDAAIDQYS
QTLRTLEARV QEGGQAQTAP APVMAPTA
//