ID A0A1N7RXZ7_9BURK Unreviewed; 1200 AA.
AC A0A1N7RXZ7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:SIT40002.1};
GN ORFNames=BN2476_230336 {ECO:0000313|EMBL:SIT40002.1};
OS Paraburkholderia piptadeniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT40002.1, ECO:0000313|Proteomes:UP000195569};
RN [1] {ECO:0000313|EMBL:SIT40002.1, ECO:0000313|Proteomes:UP000195569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 7183 {ECO:0000313|EMBL:SIT40002.1,
RC ECO:0000313|Proteomes:UP000195569};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CYGY02000023; SIT40002.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7RXZ7; -.
DR OrthoDB; 9803617at2; -.
DR Proteomes; UP000195569; Unassembled WGS sequence.
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 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 PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyruvate {ECO:0000313|EMBL:SIT40002.1}.
FT DOMAIN 635..667
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1200 AA; 130306 MW; DAFB11B2A0CDEC75 CRC64;
MTARLPIDGT PALADYRLSD NLTATRGRIF LTGTQALVRL ALMQRQLDRA RGLNTAGFIS
GYRGSPLGMV DQQLWKAKKL LDANDVRFLP AINEELGGTA VLGTQRVEAD PERTVDGVYA
MWYGKGPGVD RAGDALKHGN AYGSSQHGGV LVVAGDDHGC VSSSMPHQSD FAMMAWHMPV
VNPSNVADML EFGLYGWALS RYSGAWVGFK AISETVESGS TVDLDALQTQ WTTPEGFQAP
AGGLHNRWPD LPSLTIEQRL HAKLDAVRHF ARANSIDKWI APSPHANIGI VTCGKAHLDL
MEVLRRLDLT VADLEKAGVR IYKVGLSFPL EMTRIDAFVS GLSEVLVIEE KGPVIEQQIK
DYLYNRKQGA RPVIVGKHAE DGAMLLSSLG ELRPSRILPV FATWLAKHKP ALDRRERVVD
LVAPQILSNA ADAVKRTPYF CSGCPHNTST KVPEGSIAQA GIGCHFMASW MERDTTGLIQ
MGGEGVDWAA HSMFTKTRHV FQNLGDGTYF HSGILAIRQA VAAKATITYK ILYNDAVAMT
GGQPVDGSIS VPQIARQVEA EGVSHFVVVS DEPEKYDGHH GIFPKGTTFH HRSELDKVQR
ELRDIDGVTV LIYDQTCAAE KRRRRKKGEF PDPDKRLFIN EEVCEGCGDC GVQSNCLSVE
PVETPLGRKR RIDQSSCNKD YSCVNGFCPS FVTIEGGKLK KAAGVAFDAA ALATRVDALP
LPATQLDAAP YDILVTGVGG TGVVTVGALI SMAAHLEGKS ASVLDFMGFA QKGGSVLSFV
RFAARDEWLN QVRIDTQQAD VLLACDMVVG ASADALQTVR HGRTRIVVNT HAIPNASFVQ
NPDANLHADA LIDKMRHAAG EERMSSCDAQ ALATRFLGDT IGANILMLGF AWQLGLVPVS
FAAMMRAIEL NNVAVQMNQL AFSIGRMAAA DPAGLEALWS QRHAAQQPAV SLEKLETLDA
LVADREARLL AYGGAAYVKR YRALVGAARQ AERRLEGTQA ERLSRAVATT FYRLLAVKDE
YEVARLHSDP AFRTALEAQF EGVAGKDFGV KFNLAPPTIS RAKHGATPQK KTFGQWMWPV
FGAMAKWRGL RGTMLDPFGR TVERQMERQL STDYETTMQR TFALLNNVTA DDIVKLADLH
ARVRGYGHVK LANLAAVKRS ERELAARLHI EAATGAAVNA ALEEAKGAGT LRGIPVVVAK
//
