GenomeNet

Database: UniProt
Entry: A0A0N9NL88_9ACTN
LinkDB: A0A0N9NL88_9ACTN
Original site: A0A0N9NL88_9ACTN 
ID   A0A0N9NL88_9ACTN        Unreviewed;      1154 AA.
AC   A0A0N9NL88;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:ALG86514.1};
GN   ORFNames=ACH46_01680 {ECO:0000313|EMBL:ALG86514.1};
OS   Gordonia phthalatica.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG86514.1, ECO:0000313|Proteomes:UP000063789};
RN   [1] {ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA   Jin D., Kong X., Bai Z.;
RT   "Complete genome sequence and metabolic analysis of phthalate degradation
RT   pathway in Gordonia sp. QH-11.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALG86514.1, ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|EMBL:ALG86514.1,
RC   ECO:0000313|Proteomes:UP000063789};
RX   PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA   Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT   "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT   isolated from activated sludge.";
RL   Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
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; CP011853; ALG86514.1; -; Genomic_DNA.
DR   RefSeq; WP_062394833.1; NZ_CP011853.1.
DR   AlphaFoldDB; A0A0N9NL88; -.
DR   STRING; 1136941.ACH46_01680; -.
DR   KEGG; goq:ACH46_01680; -.
DR   PATRIC; fig|1136941.3.peg.337; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000063789; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; 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; 2-OXOGLUTARATE OXIDOREDUCTASE SUBUNIT KORB-RELATED; 1.
DR   PANTHER; PTHR48084:SF1; 2-OXOGLUTARATE SYNTHASE SUBUNIT KORB; 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:ALG86514.1}.
FT   DOMAIN          625..657
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1154 AA;  124072 MW;  2A33D5A23424A6F5 CRC64;
     MTSVADPRAQ TFDLSDKYRP NSGPVLLTGV QAIARMLVEN HERERRTGRN VASFVSGYQG
     SPLAAVDKVF GEVPDLDAHA ITFVPGLNEE LGATSVWGSQ QELPKGARTH DGIVGVWYGK
     GPGLDRASDA FRHAAMYGAH PKGGALALVG DDPAAKSSTV PAASERSLAA LSMPVLFPRN
     AEEVIAFGIF GIELSRASGT WPAMKLVADV CDGLWTLNRD FTEFHVDVPD LEWQGRPWTY
     RQRVMAAPPD SVLAEADLYG PRWEMVQKMT ALSEIDAIEV NPADAWLGIV AVGTAYDSLR
     QGLSELGLHD DDLIRAGIRI MRVGMPYPLG AEKVRQLADG VETVLVVEDK MSFVESQVVD
     VLYGTANAPR IIGKRDEQRR PLVPSDGELT AARLLRTLRH VLEGRVAVNI PKPPPPAITL
     LDTKRTAYFC SGCPHNRSTA VPDGSLAGGG IGCHTLVTMS SRTDSQVTGL TQMGGEGAQW
     IGQAPYTDVK HIFQNVGDGT YFHSGQLAVQ ACVAAGVNIT YKILFNAAVA MTGAQDAEGG
     LTVPQLTHKL KSEGVAKIIV CAEEPERHPK GSLADGVLLW DRDRLDEAQR MLRDIEGVTV
     LIYDQQCAAE ARRKRKRGTL PTPRTRVIIN EAACEGCGDC GVKSNCLSVQ PVETEFGRKT
     RIDQTSCNTD YTCMDGDCPA FVTVELPEEG TQLPKKEAAK APLVGDPEFA ALTDTHNIFL
     AGIGGTGIVT VNQVLGTAAL RAGLHVEGLD QTGLSQKAGP VTSHLRLSTE ELAASNRISP
     AGADCVLAFD LLTAADAKHV GVADPERTVT VASTSRTATG EMVYDRNVAY PEDASLLDRV
     GARARQVVSF DAAEAAEAIF GHTATANFLL VGAAYQAGAL PIPAASIEEA IAVNGVAVKA
     NQEAFRWGRV AVADPTAFAA ATASATIAHR SDDVVPTHLF VGSPLTGTVR ELVERRAAQL
     VAYSGERAAA AYIRDIERVW RRERVFTDST ELSEAVASNL HRLTAYKDEY EVARMLTDKA
     FIDSVASEVP GAGNLTYKLH PPVLRAMGRE KKIGFGPRSH VALRVLAKGK FLRGTKFDPF
     GKAEVRKIER RLLAHYRELV DGLVNNLSEA SYASSVDVAR APELVLGYED VKLRNIDRYR
     ARLGELGIDT TPIR
//
DBGET integrated database retrieval system