ID A0A0D6TFT1_9RHOB Unreviewed; 1129 AA.
AC A0A0D6TFT1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:KIX19016.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:KIX19016.1};
GN ORFNames=SY26_02505 {ECO:0000313|EMBL:KIX19016.1};
OS Paracoccus sp. 228.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1192054 {ECO:0000313|EMBL:KIX19016.1, ECO:0000313|Proteomes:UP000032743};
RN [1] {ECO:0000313|EMBL:KIX19016.1, ECO:0000313|Proteomes:UP000032743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=361 {ECO:0000313|EMBL:KIX19016.1,
RC ECO:0000313|Proteomes:UP000032743};
RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT Genomic and a Proteomic Perspective.";
RL Submitted (FEB-2015) 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:KIX19016.1}.
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DR EMBL; JYGY01000001; KIX19016.1; -; Genomic_DNA.
DR RefSeq; WP_045999126.1; NZ_JYGY01000001.1.
DR AlphaFoldDB; A0A0D6TFT1; -.
DR STRING; 1192054.SY26_02505; -.
DR PATRIC; fig|1603292.4.peg.512; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000032743; Unassembled WGS sequence.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:KIX19016.1}; Pyruvate {ECO:0000313|EMBL:KIX19016.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032743}.
FT DOMAIN 622..652
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1129 AA; 123697 MW; D1B5BE15EAC5170F CRC64;
MSKQEFSLAD RFDLSKRHVL LNGTQALVRL MLMQSARDKA AGLDTAGLVT GYRGSPLGSV
DLQMTREAKR LAAAQVLFQP GLNEDLAATA IWGSQQAELR GEGRHDGVFA LWYGKGPGVD
RSGDVMRHGN MAGSSRHGGV VMAMGDDHTG ESSTVLHQSD WAMIDAYIPV LSPAGVQEIL
DYGLYGFALS RYAGVWTGLK TMKDTVEATS VVDGDPHRMA FTLPERVLPE GGLNIRLGDT
PVAQEARMID HKRWAAEAFS RANRIDRKVW GRSGARIGFV AAGKNWLDLV HALSLLGIDE
AEAERLGLTT YKVGQTWPMD MKSIQEWSEN LELIICVEEK RKLIEVQLKE AIFDNRHGRR
VHGWKHDRTG EELFPTRYAL DPVMIAQKIG GILIEEGRGT ERLRAGLERL NEVRRNDNAP
EIATRTPWFC SGCPHNSSTT LPEGSRAYAG IGCHYMVQWM GRETEGFTHM GGEGANWIGE
APFSTRGHVF QNLGDGTYNH SGSLAIRAAL AAGTNITYKI LYNDAVAMTG GQPNEGGLTA
PQIARELVAM GVGTVVVVHD EKEDVDQAQF PKGLRFEERA QMMTVQRDLE KVAGVSAILY
VQTCAAEKRR RRKKGQFPDP DRRIFINPDV CEGCGDCSVQ SNCVSIVPLD TELGRKRQID
QSSCNKDYSC VNGFCPSFVS VKGGKLRKPK AEAFDLPDLP QPTLPTINGT HNVVITGVGG
TGVVTIGAVL AQAAHMDGKG AGMMEMAGLA QKGGAVHIHL RLAERPADIS AIRVAVGEAD
CVIGGDLVVT AGAKTVGLMT QGRTGAVVND HEIITGDFTR FRDFQVPSDR LRLSLQARLG
DRVAFFDAND LALRLLGDSI YSNMLVLGAC WQRGLIPLSL EAIMEAIRLN GAQVDANQRA
FQIGRWAVVY PEQTRKPAEV TQLPVDPVAY RAERLVGYQN KRLAARYRKL VDAAPAPLRD
SVARSYYKLL AYKDEYEVAR LHLTTAEQVA ARWEGDVTLS LHLAPPMLTG KDANGRPRKR
EFGPWMLRAF RVLARMKGLR GTPLDPFGYS AERRRERAMI REYEADMTRV FASVTDAMMP
VAIELAELPL GVRGFGPVKD KAADLAATRR AELLAQLQAG HPPIREAAE
//