ID A0A1S1QZX2_9ACTN Unreviewed; 1307 AA.
AC A0A1S1QZX2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:OHV39227.1};
GN ORFNames=BCD49_11870 {ECO:0000313|EMBL:OHV39227.1};
OS Pseudofrankia sp. EUN1h.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Pseudofrankia.
OX NCBI_TaxID=1834515 {ECO:0000313|EMBL:OHV39227.1, ECO:0000313|Proteomes:UP000179465};
RN [1] {ECO:0000313|Proteomes:UP000179465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EUN1h {ECO:0000313|Proteomes:UP000179465};
RA Ghodhbane-Gtari F., Swanson E., Gueddou A., Morris K., Hezbri K., Ktari A.,
RA Nouioui I., Abebe-Akele F., Thomas K., Gtari M., Tisa L.S.;
RT "Sequence Frankia sp. strain EUN1h.";
RL Submitted (JUL-2016) 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:OHV39227.1}.
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DR EMBL; MBLN01000042; OHV39227.1; -; Genomic_DNA.
DR Proteomes; UP000179465; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR Gene3D; 3.40.50.970; -; 2.
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; IPR002869; Pyrv_flavodox_OxRed_cen.
DR InterPro; IPR029061; THDP-binding.
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 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.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:OHV39227.1}.
FT DOMAIN 717..748
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 112..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1307 AA; 135601 MW; BB65CA06BCA95DBF CRC64;
MTTQAGGPGA AGPGQAAPAP VAAEPALLSG VEALARLLVV RAELDARAGL TTATMVSGYP
GSPLGTFDLT IERSAALLAE HRVRHRPGLN EELAAATVWG SQMGAGRSLL APRRDVAGPG
EPPAASVPGD LAADAADGGT AAGGALGGDD GAIDGVVGAW YGKTPGLDRC GDVLKHAGAM
GTGPNGGVVM FCGDDPSAKS STLACDSQYT FEDACVPVLV PGDQQDILDL GVHAFRMSRY
SGAWTGLKIV TSVADGIGTV DAGVDRHTPS DPTGHAVDGQ PWRHIPSTAV GPHAAPGQEE
QVIDLRLRAA EAYARHNRLD RVVGAPAGAR LGVVCAGKTY FDVAQALTDL GVGADRLADV
GIRMLRLAVT YPLGRETVLE FARSVDEIVV IEEKRPFVET QLRAILHEAG LTTRVAGKRA
TSQIGSADPA GTPRDGRPLV PMAGELDASK VAAVLKRVLP DLAAARVAAA TANGASNGAS
NGAPNGSPNR RLLPVVTASA PRPVITLPLV DLPARPPGFC SGCPHNRSTV FPEGALVGGG
VGCHGIMYFE ARHLGMKSLP PTPMGAEGVP WLGLSPFVDE PHLIQNLGDG TLSHSGILAI
RASVAGGVNV TFKILYNTAV AMTGGQDVVG LMDVPAMTRA LEAEGVSRVV VCAEDPKHYG
RRARFAPGVR VLGRDHLEEV QEELRSVPGV TVVIYDQRCA AESRRLRKRG LLPEPPRRVV
INEAVCEGCG DCSVKSNCLS VLPHHTEFGE KRRVDDLSCN RDYTCLEGDC PSFVTITPRE
PGLFARLRPG RSGTGSAGKK AAEHVRPHLP AGGLPEPDVQ PITESFGVYF TGVGGTGVVT
ANRVIASAAQ AAGLAVGGLD QTGLSQKAGA VVSHLRLSPK RAGGLDAAAG ASTVGEGGAD
LYLSGDILQA AAAKHLATVQ PGRTVAVVDV TVTPTAAMLQ RDIAAPDEAV MRAAIAERVG
DGRALFLDSK RIAEQVFANQ LLGNIVLLGA AYQLGGLPLP LADLEKAMGR TGKAAADNRE
AFAWGRWVAH DLAAVEAALA ATAGTDAGAG AGAGAVVATA TAKPSIFDPS PGAVATAGRL
VAEGDLPAEL PDDLRALLVR RAAQAIDYQD AARATRFLGL VATAAGRDAA DHGWALTRAV
AESWFKLLTY KDEYEVARLH LLADHAQTAA DLGIDGPYKV TYHLHPPSLR RMGLKHKLPA
ARPWAVMFHG LRTMRRLRGT PFDIFGLDRD RRLERAVIKE YEALVTGNLT AGRPYADLVT
LAESAQMIKG YESIKAAAVD RWRAQVAQLA PAEPAEPAEQ VTVGGNA
//