ID   B3QK71_RHOPT            Unreviewed;      1155 AA.
AC   B3QK71;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:ACF00088.1};
DE            EC=1.2.7.8 {ECO:0000313|EMBL:ACF00088.1};
GN   OrderedLocusNames=Rpal_1554 {ECO:0000313|EMBL:ACF00088.1};
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960 {ECO:0000313|EMBL:ACF00088.1, ECO:0000313|Proteomes:UP000001725};
RN   [1] {ECO:0000313|EMBL:ACF00088.1, ECO:0000313|Proteomes:UP000001725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1 {ECO:0000313|EMBL:ACF00088.1,
RC   ECO:0000313|Proteomes:UP000001725};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001096; ACF00088.1; -; Genomic_DNA.
DR   RefSeq; WP_012495014.1; NC_011004.1.
DR   AlphaFoldDB; B3QK71; -.
DR   KEGG; rpt:Rpal_1554; -.
DR   HOGENOM; CLU_009166_1_0_5; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000001725; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd07034; TPP_PYR_PFOR_IOR-alpha_like; 1.
DR   Gene3D; 3.40.50.920; -; 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   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   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   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ACF00088.1}; Pyruvate {ECO:0000313|EMBL:ACF00088.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          449..593
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   DOMAIN          722..901
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          935..1134
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1155 AA;  124148 MW;  E28BCBDB91256FFF CRC64;
     MTEPSKLPNV TLSDKYEQPE GEVFLSGNQA LVRLVLQQRA RDAATGLNTA GFVSGYRGSP
     LGRLDMELWQ SGDLLHKAQV KFQPGVNEDL AATAVWGSQQ VGSFAGARYD GVFGIWYGKG
     PGVDRSGDAI KHANAAGVAP LGGVLALAGD DHGAKSSTQA HQSDYAFIAA GIPVLYPANV
     QEILDYGLHG LAMSRHAGCW VALKLVTDVV EGSSSVRVGL DSPAIVVPSQ PAGDVHIKRI
     AMPKAQEEAL YRLRLPAAMA YARANALNRI VAAAPDARIG VVTAGKSYAD TRAALDRLGG
     RDGFHPDSVR LLKIGMVWPL DPEIVRQFAR GLDTILVVEE KRPLLEDQIK AILFDDAAGP
     RPRVIGKFVG VSAWDAGRGT EVFAMTGELS PDLIATRIAD GLRLSPASAP SRALALANAT
     TPERAPTFCS GCPHSTSTRL PDGSLALAGI GCHSIALLQN PMRTGPLAHM GAEGVMWVGM
     APFTDMPHVF ANMGDGTYFH SGFLAIRQAI AAKSTITYKV LVNGFVSMTG GQPIEGELTP
     AQLATELLTE GVAKVVVVAD DPQKYQGVAL PVGVRVEHRE RLELVQKELR EVAGVSVLIY
     DQMCATERRR QRKRGKMPDP GTRTFINSAV CEGCGDCGEA SNCLSVEPLE TDYGRKRRIN
     QASCNKDLSC VQGFCPSFVT VVGGSLRKPV KTAPRAATTE TLPEPVLPTL ADPIGVIVAG
     VGGTGVITLG AVIGMAAHLD GIAVSTLDLT GLAQKYGAVT SHIRLARTPD RLSTHRLADG
     DADVAIGADL IVAAGAETVA KLDAARTRTV VDAAINPTRD FSVDPDWSVD DRALIGRLEA
     ATRETLALEA TEIARRLVGD PLGANMLLLG FAWQKGWLPL SRAALEQAIR LNAVAVDLNL
     TSFGWGRALA HDPAMVRAAA FPPVQQPTAA ANDTLDELVA RRAADLTDYQ NAALAESYRA
     FVAKVADREQ RLGQGNALAR AVARNYYKLL AVKDEYEVAR LYTSLAFRRE LEQTFDGEFT
     LRFHLGAGPF ARHVDGIATP KKTEVGPWMM KAFHVLAALR RLRGSLLDPF RNNPERRLAD
     RERDRYEADL DRLIAELDAD RLGVAVEIAS LPDKLRGYGH VRERAADDVQ QRREALWRRW
     EHRRSEPARE KEAAL
//