ID   A0A167GBF4_9BURK        Unreviewed;      1194 AA.
AC   A0A167GBF4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:AOW15133.1};
GN   ORFNames=LPB072_22315 {ECO:0000313|EMBL:AOW15133.1}, LPB72_21700
GN   {ECO:0000313|EMBL:OAD39223.1};
OS   Hydrogenophaga crassostreae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1763535 {ECO:0000313|EMBL:AOW15133.1, ECO:0000313|Proteomes:UP000185680};
RN   [1] {ECO:0000313|EMBL:OAD39223.1, ECO:0000313|Proteomes:UP000185657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0072 {ECO:0000313|EMBL:OAD39223.1,
RC   ECO:0000313|Proteomes:UP000185657};
RA   Shin S.-K., Yi H.;
RT   "Draft genome sequence of Hydrogenophaga sp. LPB0072.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AOW15133.1, ECO:0000313|Proteomes:UP000185680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0072 {ECO:0000313|EMBL:AOW15133.1,
RC   ECO:0000313|Proteomes:UP000185680};
RA   Kim E., Yi H.;
RT   "Hydorgenophaga sp. LPB0072 isolated from gastropod.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP017476; AOW15133.1; -; Genomic_DNA.
DR   EMBL; LVWD01000043; OAD39223.1; -; Genomic_DNA.
DR   RefSeq; WP_066096360.1; NZ_LVWD01000043.1.
DR   AlphaFoldDB; A0A167GBF4; -.
DR   STRING; 1763535.LPB072_22315; -.
DR   KEGG; hyl:LPB072_22315; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000185657; Unassembled WGS sequence.
DR   Proteomes; UP000185680; Chromosome.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
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; 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.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:AOW15133.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185680}.
FT   DOMAIN          487..591
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          764..951
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          981..1177
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1194 AA;  130253 MW;  95280E0180F8781A CRC64;
     MNAPLPEHIR RALETVTLDD KYSLDHGRAF MSGVQALVKL PMLQRQRDAL QGKNTGGFIS
     GYRGSPLGGY DQALQKAEPY LKAQNIVFQP GVNEELAATA LWGTQQLGFA PEGSNKFDGV
     FGIWYGKGPG VDRCSDVFKH ANMAGTTPWG GVIAVAGDDH ISKSSTAAHQ SDHIFKACGL
     PVFFPTSVQD ILDLGIHAIA MSRFSGVWAG MKTIQEIVES SATAIIDPER INIVVPEFDM
     PPGGVHIRWP DAALEQEARL FDYKWYAALA YIRANKLNHN VIAGPHDRFG VIASGKAYND
     TRQALLDLGL DDATCQRIGL RLHKVAVVWP LEAQTTREFA TGLHEILVVE EKRQVIEYQL
     KEELYNWRAD VRPNILGKFD EVEGDFTGGE WSMPNPSAHH LLRANADLNP AIIARAIAKR
     LRKLGVPEDV QARIDTQLAI LTAQEQSMQT LLTKGVDGAE RQPWFCSGCP HNTSTKVPEG
     SRAMAGIGCH FMTIWMDRAT VGFTQMGGEG VPWMGQQPFS NDQHMFANLG DGTYFHSGIL
     AIRQSIAAGV NITYKVLYND AVAMTGGQQV GERPEGHSVV QIAQSMRAEG AVKIIIVTDE
     PEKYDSITGL PSGIAIQHRD TLDAVQREFR EIKGTTVIIY DQTCATEKRR RRKRGTMVEP
     TERVIINELV CEGCGDCGVQ SNCLSVEPLE TEFGRKRTIN QSSCNKDFSC VKGFCPSFVT
     VDGGKLRKKG QGADKPVWTG GDVPEPALPR LGAEAWGVIV AGVGGTGVIT IGQLLGMAAH
     MEGKGIVTQD AAGLAQKGGA TWSHVLIGAR QEDIRTTRVG SASADLVIGC DPLVAANKET
     WQRLRAGRSH VALNANATPT AAFVTNIDWQ NPAQACVDTL VSNLGTDDVG VLDAETAASK
     LMGDSIYTNP MMLGYAWQRG WVPLAFASLM RAIELNGVQV ANNKTAFEWG RRAAHDPQAF
     AGLLSGGGAK VIQFKPRETV ATVIERRVAF LTDYQNAAYA ADYLRFVDRV RKVEAALGKS
     DLTMAVARNL FKLMAYKDEY EVARLHSDKA FHERIASQFE GDYKLRVHLA PPLTAKKNAK
     GELIKKAYGP FMFTAFGWLA KFKGLRGTAL DVFGYTDERR TERALIAEYR TAIEGLLSDL
     DAGNLALALD IARVPDLIKG YGHVKDRNLA AARSRWADLQ ARWAAGESAE ARVA
//