ID A0A1H3L192_9RHOB Unreviewed; 1139 AA.
AC A0A1H3L192;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:SDY58151.1};
GN ORFNames=SAMN05444486_102882 {ECO:0000313|EMBL:SDY58151.1};
OS Lentibacter algarum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Lentibacter.
OX NCBI_TaxID=576131 {ECO:0000313|EMBL:SDY58151.1, ECO:0000313|Proteomes:UP000199026};
RN [1] {ECO:0000313|EMBL:SDY58151.1, ECO:0000313|Proteomes:UP000199026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24677 {ECO:0000313|EMBL:SDY58151.1,
RC ECO:0000313|Proteomes:UP000199026};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNPR01000002; SDY58151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3L192; -.
DR STRING; 576131.SAMN05444486_102882; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000199026; Unassembled WGS sequence.
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; 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; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR48084; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR PANTHER; PTHR48084:SF1; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORB; 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 PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:SDY58151.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199026}.
FT DOMAIN 626..655
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1139 AA; 124207 MW; BBDF2C4D99529CA5 CRC64;
MSDQKVSLND RFDLTKSPVL LNGTQALVRL MLTQKERDRA AGFATAGYVT GYRGSPLGAV
DMQMSRAEKI LTENDVKFQA GLNEDLAATA LWGSQQAELR GEGKFDGVFG LWYGKGPGVD
RSGDVFRHAN MAGTSAKGGV LVAMGDDHTG ESSTVLHQSE WALIDAYMPI VSPAGVQEVI
DYGVYGWALS RFAGLWVGLK TMKDTIEATA VVDGDPNRVN LVLPEFDMPQ GGLNIRLVDT
PHEQEARMID YKRFAAEAFS HANKMDKRVW GKAGAKIGFV AAGKNWLDLC HALSLLGIDE
AEAERLGVTT YKVGQTFPLD MRGFSDWADG LDLIVVVEEK RKLIEVQIKE ALFDVRKGRR
VYGWYKGGAG GIHREELFPT RGALDPVWIA EKLGDILVEE GRGTDGVKAG LARIAEARRA
DNAEDIAARL PYFCAGCPHN SSTKVPDGSR AYAGIGCHYM VQWMDRNTLG STQMGGEGAN
WIGEAPFSTR AHVFQNLGDG TYNHSGIQAI RAALAAGTNI TYKVLYNDAV AMTGGQSNEG
ELDAPKIVAE LKAMGVKDLA IVYDDKEDVD MNLFPQDIEI KSREHLMEVQ ERMEAAEGVS
AIVYIQTCAA EKRRRRKRGL FPDPDKRVFI NTDVCEGCGD CGVQSNCVAI TPVETELGRK
RAIDQSACNK DFSCLKGFCP SFVTLEGATP KKAATATLEL PDMPMPELPT IVGTHNVVIT
GVGGTGVVTI GAVLAQAAQI DGKGAGMMEM AGLAQKGGAV HIHCRIAEKP SDITAIRVAT
GEAHVLIGGD MVVSAGAKTL GLTRTGQTGA VVNAHQTTTG DFTRDTEFKL PFDRLELQLE
ARLKDRLSLF DASDLAKVLL GDSIFSNMMV FGGAWQRGFV PVSYEAIMAA IGLNGAAVER
NQRAFDLGRW AVLYPDEAHR FITSTVESKS LSLKEKIDFR AGKLVDYQNA ALASQYRTFV
DRFQDEHLKE AVAKGYHKLL AYKDEYEVAR LLLSSQEKAE AEFDGDFKMS YHMAPPLLSK
FGHDGRPQKR QFGPGMKRWL KLLAKMKGLR GTPFDLFGRT EERKMERSLI AQYERDMGEV
LQKVRPETLD IAVALAELPL KIRGFGPVKA QNEAKAAKER EALLQQLRSG GAPLLKAAE
//