ID A0A0F7JWB3_9GAMM Unreviewed; 1150 AA.
AC A0A0F7JWB3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:AKH19947.1};
DE EC=1.2.7.8 {ECO:0000313|EMBL:AKH19947.1};
GN ORFNames=AAY24_05830 {ECO:0000313|EMBL:AKH19947.1};
OS Sedimenticola thiotaurini.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH19947.1, ECO:0000313|Proteomes:UP000034410};
RN [1] {ECO:0000313|EMBL:AKH19947.1, ECO:0000313|Proteomes:UP000034410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH19947.1,
RC ECO:0000313|Proteomes:UP000034410};
RX PubMed=26089430;
RA Flood B.E., Jones D.S., Bailey J.V.;
RT "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL Genome Announc. 3:e00671-15(2015).
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DR EMBL; CP011412; AKH19947.1; -; Genomic_DNA.
DR RefSeq; WP_046858882.1; NZ_CP011412.1.
DR AlphaFoldDB; A0A0F7JWB3; -.
DR KEGG; seds:AAY24_05830; -.
DR PATRIC; fig|1543721.4.peg.1207; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000034410; Chromosome.
DR GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
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 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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AKH19947.1}; Pyruvate {ECO:0000313|EMBL:AKH19947.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034410}.
FT DOMAIN 724..908
FT /note="Pyruvate/ketoisovalerate oxidoreductase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01558"
FT DOMAIN 935..1133
FT /note="DUF6537"
FT /evidence="ECO:0000259|Pfam:PF20169"
SQ SEQUENCE 1150 AA; 127142 MW; 335CC2E7CD125A87 CRC64;
MALADIKLDD KYTLDTGRVY LTGVQALTRL PMLQQQRDQQ AGLNTAGFIS GYRGSPLGGL
DKELWKAGKY LDQHHINFQP GLNEDMAATA VWGTQQVNLF EGARYDGVFS MWYGKGPGID
RSGDVFKHAN AAGTSPHGGV LVIAGDDHNS KSSTLPHQTE YAFMDAMIPV LNPAGVQEIL
DYGQIGWALS RYSGCWVALK TIAETVDTSA SVSIDPKRVQ ITIPDDYELP EGGLNIRWPH
TPLEQESLQH RHRLYAALAF ARVNKLNRIV IDTPTPRLGI ATTGKSYLDV MQALEDLGIT
PTMAAQIGIR LYKIGMSWPL EREGVRQFAE GLDEILVVEE KRGLIENQIK EQLYNWKEAV
RPKIVGKFDE SNQWLLPSAG ELTPARIARV IAARIERFHQ SEVIEKRLHF LQKKEAELAL
PRVTLDRVPH FCSGCPHNTS TLLPEGSRAT GGIGCHYMAT WMDRGTDTFT QMGGEGVPWI
GQAPFTDTPH IFANLGEGTY FHSGVLAIRA ALAANVNITY KILYNDAVAM TGGQPVDGSF
SVQQLSRQLA AEGVKRIALV SDDPDKFKDR TEFAPDTTFD HRDNLEKVQR ELRETPGVSV
LIYEQTCAAE KRRRRKRGLL NDPKVRPFIN SAICENCGDC STQSNCLSII PVETEFGRKR
AIDQSSCNKD MRCVEGYCPS FVTVHGGQLK RVASQPDGLE WPDLPLPELP GLERPHNILL
TGIGGTGVVT IGALLGMAAH IDGRGVTVLD MTGLAQKYGA VVSHIRIAVK PEDIHAMRIA
AGQADTLLAC DLAVATGFEA MAKLNPERTD AVINSHQAMT SGFIKQKDLT FPAPALEAQL
EKTTRHAQFI NASQLAESLL GDAIGANLFM VGFAWQKGYL PLSLEALKKA IELNGVSIQD
NLRALLWGRR AAVDLEAVQQ LAAPDKPAVA APKTLDELIA HRSQHLTDHQ NAAYARRYRQ
LVERVREREQ VLGLSGLTEA VAENYARLLA YKDEYEVARL YSDRAFREQI ANQFEGDFHL
EFHFDPPILS KADPETGKHR KRRFGPWMLK MLGLLRHLKV LRGSRLDPFG NNPDRQLERA
LIEDYETTLE TLLSGLNRDN LETAIALARL PEEIRGFGHV KQAAAEQAAI RQQALLNQLL
GNTLEAQQAA
//