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Database: UniProt
Entry: A0A1K1TYI1_9GAMM
LinkDB: A0A1K1TYI1_9GAMM
Original site: A0A1K1TYI1_9GAMM 
ID   A0A1K1TYI1_9GAMM        Unreviewed;      1170 AA.
AC   A0A1K1TYI1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:SFX05576.1};
GN   ORFNames=SAMN02745752_00366 {ECO:0000313|EMBL:SFX05576.1};
OS   Marinospirillum alkaliphilum DSM 21637.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinospirillum.
OX   NCBI_TaxID=1122209 {ECO:0000313|EMBL:SFX05576.1, ECO:0000313|Proteomes:UP000182350};
RN   [1] {ECO:0000313|EMBL:SFX05576.1, ECO:0000313|Proteomes:UP000182350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21637 {ECO:0000313|EMBL:SFX05576.1,
RC   ECO:0000313|Proteomes:UP000182350};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FPJW01000001; SFX05576.1; -; Genomic_DNA.
DR   RefSeq; WP_072324595.1; NZ_FPJW01000001.1.
DR   AlphaFoldDB; A0A1K1TYI1; -.
DR   STRING; 1122209.SAMN02745752_00366; -.
DR   Proteomes; UP000182350; Unassembled WGS sequence.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
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   Pyruvate {ECO:0000313|EMBL:SFX05576.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182350}.
FT   DOMAIN          734..920
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          945..1152
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1170 AA;  129461 MW;  D60B39397E83D613 CRC64;
     MNIPQPTAGQ PHLDDYRLED RYTRDQGRVF LTGTQALVRI ALRQAELDRK KGLKTGGMIS
     GYRGSPLGAV DLELWKARKL LDNHQIEFIP AINEDLAATL LLGTQQVETD PERQVDGVFG
     LWYGKGPGVD RSGDALKHGN AYGSSPHGGV LVVAGDDHGC VSSSMPHQSD VAFMSWFMPV
     IHPASVAEYE SFGLWGYALS RYSGCWVGFK AVSETVESAA SVEVPPLPEF VIPDDFTPPA
     DGLHYRWPDL PGPQLETRME HKLAAVQAFA RANPLDRRIL NLPHARFGLV TTGKAHLDLM
     EALQLLGLDE TRLRELGIDI YKVAMVWPLN RQGALDFVHG KQEILVVEEK RGIIESQIKE
     YMSEPDHPGE VLVTGKQDEQ GQPLIPYVGV LSPLLLAEFV ALRLERFFGL KFSDQLEALK
     ANCLKAQDPG GARRLPYFCS GCPHNTSTKV PEGSKALAGI GCHFMASWMG RQTESLIQMG
     GEGVNWVGRS RFTGKGHIFQ NLGEGTWFHS GSMAVRQAVA AGVNITYKIL FNDAVAMTGG
     QPVDGPVSVP MIARQSLDEG VKKVVVVTDE PEKYRREHLP AGISVHHRDE LDSLQRKLRD
     IPGCTVLIYD QACAAEKRRR RKRGLYPDPA RRVMINPHVC EACGDCSVQS NCLSVVPRET
     PLGRKRQIDQ SSCNKDFSCV QGFCPSFVTI EGGQLRKGEG LTVDAAFQQR IAALPQPQPP
     SLEQTYNLLV CGVGGTGVIT VGQLITMAAH LEGKGSSVLD FMGFAQKGGS VISFIRLAPS
     PQHLHQVRIE NGQTHALLAC DLLVATSART LPLLQPGKTR MVCNEAELPS ADYVLQRDAS
     MGVAQRLALL RSTAPASGFA SLQANRLAER LMGDSVYANV LLLGYAWQQG LLPVSESALL
     RAIELNAVAV DLNKQAFAWG RLAAAEPEQV EQLQDHQPLP ETASLQERIQ HHAGYLTHWQ
     HQAWADQYQQ QLERVRQAEM QLLQITDTTE NPSLPLTEAV ARQLFRLMSY KDEYEVARLF
     TRSDFLDEVN QTFTGHWQLH FHMAPPLLNF GKDAAGRPKK RRYGRWLLPV LRLLANLKGL
     RNTALDPFRF SQDRKLDRQL LTDYQQLLDD LLQGLKPDNH TTAVALARLP EEIRGFGPVR
     EAAAHQVQAR KEKLLREFRE GKTTTLAIAV
//
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