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
//