ID A0A1V0GWC2_9RHOB Unreviewed; 1132 AA.
AC A0A1V0GWC2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase family protein {ECO:0000313|EMBL:ARC37959.1};
GN ORFNames=A6J80_17780 {ECO:0000313|EMBL:ARC37959.1};
OS Paracoccus yeei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC37959.1, ECO:0000313|Proteomes:UP000191257};
RN [1] {ECO:0000313|Proteomes:UP000191257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA Geyer C., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP020442; ARC37959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0GWC2; -.
DR STRING; 147645.A6J80_17780; -.
DR KEGG; pye:A6J80_17780; -.
DR eggNOG; COG1014; Bacteria.
DR eggNOG; COG4231; Bacteria.
DR Proteomes; UP000191257; Chromosome.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; 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; 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:ARC37959.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000191257}.
FT DOMAIN 622..652
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1132 AA; 123119 MW; C9F329035946433F CRC64;
MSVQEFSLSD RLDLSHRHVL LNGTQALVRL MLMQAARDHA AGLNTAGLVT GYRGSPLGGV
DLQMMKSRDA LTAAKVLFQP GLNEDLAATA IWGSQQAELR GEGKYDGVFA LWYGKGPGVD
RSGDVMRHAN MAGSSRLGGV VMAMGDDHTG ESSTVLHQSD WALVDAYIPV LSPAGVQEIL
DFGLYGFALS RFAGVWTGLK TMKDTVEATS VVDGDAFRLR FVTPDFAMPP GGLNIRLGDT
PVAQEARMID HKRFAAEAFS RANRLDRPVW NHRGARIGFV AAGKNWLDLV HALSLLGIDE
PEAERLGIST YKVGQTWPMD MKSFQEWSEK LEIIVVVEEK RKLIEVQVKE AIFDNRHGRR
VLGWKHDRTG EELFPTRYAL DPVMIAEKLG AILIEEGRGT EGVRAGLRRL AEVRRNDNAP
ELAVRTPWFC SGCPHNTSTH LPEGARAYAG IGCHYMVQWM GRETVGFTHM GGEGANWIGE
GPFSKRRHVF QNLGDGTYNH SGSLAIRAAK AAGANITYKI LFNDAVAMTG GQPNEGGLTA
QQIVRELQAM GVSPVIVVHD EKEQIDRAAF PKGLRFEERA AMQAVQKELE DVPGVSAIVY
VQTCAAEKRR RRKRGAFPDP DRRIWINPEV CEGCGDCGVQ SNCVSIVPRD TELGRKRAID
QSSCNKDYSC VRGFCPSFVS VRGAVPRRPP AQALDLPDLP APALPTIRGT HNLVITGVGG
TGVVTVGAVL AQAAHIDGKG AGMMEMAGLA QKGGAVHIHL RLADRPEDIS AIRVAVGEAD
CIIGGDLVVT AGSKTIGLMA PGRTGAVVNE HEIVTGEFTR NRDFQIPGDR LKLSLQARLG
GKVVFLDAST LALRLLGDSI YSNMLVLGAA WQQGLIPLTE AAILKAIDLN GAKVAENRRA
FQIGRWAVVH PQEAARLAEG PNVTALQVDP VEYRARRLVD YQDRALAERF RALVALAPPD
LRDSVALGYY KLLAYKDEYE VARLHLASAA AVAAEFEGDA RISFHLAPPV LPGRDPDGRP
RKREFGAWMV PVFRVLAGMK RLRGSVLDPF GWLPERRAER AAIAEYEADM RRWLPTVTPA
NLALVRELAE LPLTVRGYGP VKEDAAKAAR ARRAELLDAL HRGGAPMAQA AE
//
