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Database: UniProt
Entry: A0A1H2WXF1_9RHOB
LinkDB: A0A1H2WXF1_9RHOB
Original site: A0A1H2WXF1_9RHOB 
ID   A0A1H2WXF1_9RHOB        Unreviewed;      1146 AA.
AC   A0A1H2WXF1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:SDW85290.1};
GN   ORFNames=SAMN05444336_102531 {ECO:0000313|EMBL:SDW85290.1};
OS   Albimonas donghaensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Albimonas.
OX   NCBI_TaxID=356660 {ECO:0000313|EMBL:SDW85290.1, ECO:0000313|Proteomes:UP000199118};
RN   [1] {ECO:0000313|EMBL:SDW85290.1, ECO:0000313|Proteomes:UP000199118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17890 {ECO:0000313|EMBL:SDW85290.1,
RC   ECO:0000313|Proteomes:UP000199118};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNMZ01000002; SDW85290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2WXF1; -.
DR   STRING; 356660.SAMN05444336_102531; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000199118; 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   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; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
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   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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:SDW85290.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199118}.
FT   DOMAIN          723..909
FT                   /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01558"
FT   DOMAIN          937..1136
FT                   /note="DUF6537"
FT                   /evidence="ECO:0000259|Pfam:PF20169"
SQ   SEQUENCE   1146 AA;  123037 MW;  69A6F1F316093C24 CRC64;
     MAPLDAQVAL TDKYRVSRGA ALMNGMQALV RLVIEQADAD KDAGWKTGGY VSGYRGSPIG
     GFDMELMRAS AELEERNVVF NPGLNEDLAA TAIAGTQTLG VVDDPEVEGV FSLWYGKGPG
     VDRSLDAIKH AALAGASPRG GLMFLLGDDP VSKSSTTAHQ SETAMMHVQV PVLYPASVHE
     YVPLGLHGIA MSRHTGAATS LKIVTDTADS TATVALDRLR PENIVYPTLP GFELPLHNTG
     TLLPYVAQER RMGVRLQACM DYAYANKLNE AVFQPSGQKR LGIVAVGKGY VDAMSGLRML
     DLDADRAAAA GIGMFRMRMT WPVEPKSLME FVQGYDQILV IEEKRGIVED ALARMLVNLP
     GPRPLVTGKL DAQGAPLTQD WGELQPDTVA EVISREACGM GLIEATPPAP PRLTGNAPTA
     PRTPYFCAGC PHNRSTKLPD GSLAGGGIGC HAMSVMHDSL NTQIFTQMGG EGMHWVGRAN
     FAGRKHMFQN IGDGTFTHSG LLAVRAAVAS GVNITYKLLY NDAVAMTGGQ VMEGQPLPSD
     MARQVLSVGV KRVVVVSDDV EATKETGDWP SANVSFHDRS EHILVQTQLR EEEGTTVLLY
     VQTCAAEKRR RRKRGKFADP PKRVVINPLV CEGCGDCGIQ SNCVAVKPLD TPFGVKRRVD
     QTACNKDYSC LEGFCPSFVT VEGEESDPLL GKKGIRHQPP EDALPEPTIA PPADWGALIT
     GIGGTGVVTV AAVLGMAARL EGLHSLALDQ TGLSQKNGAV QSHLQIGPLP IDDRPARVGR
     GKGKLLLACD MLVGAGDEAM ALLDPAEGRA IANAEVEPLP MFAKDPNARP DAGQLSARLT
     QHLGESRVMV QDVKHLATAL VGDGMGANLM LVGVACQAGT LPVTPEAIER AIKLNGAAVE
     MNLAAFRWGR WIAHDPARAE AAAGEKKLPS WLTEDYDALV ARFESYLTDY QSARYARKFR
     EALAKVEAAE EAAWPGRRDL SRLAARALHK SMAIKDEYEV ARLHRHPDWL AQLGRDYAPD
     ARVSTWLAPP MLAKTDPLTG HPKKKAFGPW VQKAFGTLAG MKALRGTPLD VFGRTEERKS
     ERALVGETFK LVDLVAGKLS PATEARCREA LSLPLEIKGF GHVKAANQAR VKPEWDRLVA
     DLSSIA
//
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