ID A0A2U8GK95_9RHOO Unreviewed; 1200 AA.
AC A0A2U8GK95;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Pyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:AWI73844.1};
GN ORFNames=CEW83_00230 {ECO:0000313|EMBL:AWI73844.1};
OS Parazoarcus communis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Parazoarcus.
OX NCBI_TaxID=41977 {ECO:0000313|EMBL:AWI73844.1, ECO:0000313|Proteomes:UP000244930};
RN [1] {ECO:0000313|EMBL:AWI73844.1, ECO:0000313|Proteomes:UP000244930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSPY31 {ECO:0000313|EMBL:AWI73844.1,
RC ECO:0000313|Proteomes:UP000244930};
RA Woo J.-H., Kim H.-S.;
RT "Azoarcus.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP022187; AWI73844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U8GK95; -.
DR KEGG; acom:CEW83_00230; -.
DR Proteomes; UP000244930; Chromosome.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR CDD; cd02008; TPP_IOR_alpha; 1.
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; 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 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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:AWI73844.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244930}.
FT DOMAIN 743..930
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 962..1161
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1200 AA; 129556 MW; AA838A683FE16B31 CRC64;
MNTLTVAAAT PVTAVNRDYR LADNLEAVRG QVFLTGTQAL VRLPLMQAAL DRAAGLNTGG
FISGYRGSPL GAYDQQLWKV RPLLDANRIR FLPAVNEELG ATAVLGSQQV ERDEARTVDG
VFAIWYGKGP GVDRAGDALR HGNAYGASPH GGVLAVIGDD HGCVSSSMPH QSDFTLQAWS
LPVLNPASVA EMIEFGLYGW ALSRFSGCWV GLKAISEMVE SGSTVDLDAI RARFEAPADY
TPPEGGLHYR WPDLPNLVIE QRLAAKLDAA RHFARHNSID RLLCPATLAD VGIVTCGKAH
LDLLEALRRL GLGMDDLEAN GIRLYKVGQS FPLEPGRMRA FAAGLKEILV VEEKGPFVEQ
QIKNLFYNDD PARRPQVFGK TAQCGAPLLS ALGELRPSRV MPVLADWLAR HRPVLDRREH
VEDFTAPTLL SNAADGVRRV PYFCSGCPHN TSTRVPEGSH AQAGIGCHFM ASWMPDRETT
GLIQMGGEGV DWVAHSGFTR TPHVFQNLGD GTYFHSGFLA IRQAIAARTN VTYKILYNDA
VAMTGGQPVD GTVTVDAIAR QVEAEGARRV VVVSDEPEKF KGHEGQFPRG TSFHHRSELD
TVQRELREVK GVSVLIYDQT CAAEKRRRRK KKAYPDPDRR LFINAAVCEG CGDCGKQSNC
LSIVPLDTPL GRKRMIDQSS CNKDYSCVEG FCPSFVSVIG GKVRKAVGAS FDEDRLQARV
AALALPAKHE WSGPYDLLVT GVGGTGVVTV GALVTMAAHL EGKSASVLDF MGFAQKGGQV
LSFVRMATDP GALNQVRIDT QQADAVIACD LVVGASNDAL QTIKHGRTRV VANLHEIQTA
KFVLDPEADL HVEALLEKIR YAAGAAQLST CDAQALSVRM LGDTIGANIL LLGFAWQQGL
VPVSLEALGR AIELNGVAVA TNLTAFSLGR LAAGDPQGLA ALAGSTPNSA VQPDEGQGES
LAALVDARVA MLTVYQSAAY ATQYRALVDE VERAERKLVG ELGVLRLSPV VARVHARLLA
IKDEYEVARL FTDGQFDAAL NEQFEGDFSL QFHMAPPLLS RPGPSGRPRK LAFGPRLMPL
LRLLARAKVV RGTVLDIFGR SEERRMEREL AADYARTIRA LLPRLTSVNM SQAIELAGLA
DGIRGFGPVK LANLRRIKQQ ERTLVHALGL DFVAGPTVSH LCEPVRGRAA LHAISVVKAP
//
