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Database: UniProt
Entry: A6GQS6_9BURK
LinkDB: A6GQS6_9BURK
Original site: A6GQS6_9BURK 
ID   A6GQS6_9BURK            Unreviewed;      1196 AA.
AC   A6GQS6;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=Indolepyruvate ferredoxin oxidoreductase {ECO:0000313|EMBL:EDM83479.1};
DE            EC=1.2.7.8 {ECO:0000313|EMBL:EDM83479.1};
GN   ORFNames=LMED105_09292 {ECO:0000313|EMBL:EDM83479.1};
OS   Limnobacter sp. MED105.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Limnobacter.
OX   NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM83479.1, ECO:0000313|Proteomes:UP000010322};
RN   [1] {ECO:0000313|EMBL:EDM83479.1, ECO:0000313|Proteomes:UP000010322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED105 {ECO:0000313|EMBL:EDM83479.1,
RC   ECO:0000313|Proteomes:UP000010322};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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:EDM83479.1}.
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DR   EMBL; ABCT01000007; EDM83479.1; -; Genomic_DNA.
DR   RefSeq; WP_008250251.1; NZ_ABCT01000007.1.
DR   AlphaFoldDB; A6GQS6; -.
DR   STRING; 391597.LMED105_09292; -.
DR   OrthoDB; 9803617at2; -.
DR   Proteomes; UP000010322; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0043805; F:indolepyruvate ferredoxin oxidoreductase activity; IEA:UniProtKB-EC.
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   InterPro; IPR009014; Transketo_C/PFOR_II.
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   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:EDM83479.1}; Pyruvate {ECO:0000313|EMBL:EDM83479.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010322}.
FT   DOMAIN          660..692
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1196 AA;  132509 MW;  B79871949B47F7D7 CRC64;
     MNAPQYPLYR AVTLSDKYTL SQGKIYLTGT QALVRLMLLQ SQLDRMNGLN TGGFVSGYRG
     SPLGGVDQAF WAAQQFLKPA NIHFQAGVNE DLAATAVWGS QQLNLFQGAT VDGVFGLWYG
     KGPGVDRSLD VFKHANAAGT SKHGGVLLVA GDDHAAKSST LPHQSDHVLK AAMIPVLFPS
     NVQEILDFGV LGYAMSRYAG VWVGMKAVAD VVECSATVDI DPKRYQFELP GDFTMPEGDL
     NIRWPDTALA QEARLIDHKL YAALAFCRAN GINKTVIDSP VARFGIVATG KAFQDTLQAL
     SDLGLNPQRC TEIGLRVYKV GMVWPLDAVG IREFSRGLQE ILVIEEKRQF VEYQIKEELY
     AWREDVRPKV YGKFDERLSE DGREGGEWSL PQGNWLLPSH YELDPALIAV AIAKRLRHMQ
     LPADIKTLID NRIATIEHSH EVGHSAHLPV ERKPYFCSGC PHNTSTKVPE GSRAMAGIGC
     HYMAVWMDRN TQTYTQMGGE GVPWIGQAPF THTQHVFANL GDGTYFHSGI LAIRASIAAG
     VNITYKLLYN DAVAMTGGQH LDGTLTVPQL TRQLAAEGVA KIVVVSDNPA LHLRNLPNDP
     KAEGTEVFHR RDMDTVQRLL REIQGTTVLI YEQTCASEKR RRRKRTDPVT GQLQFPNPPK
     RVLINPRVCE GCGDCSKHSN CLSIEPVSTP WGVKRTINQS TCNKDYSCLE GLCPSLVTVE
     GGELRKPDVS THHSALVKVC ESLAEPQYHI HPDELDQRYA VLINGVGGTG VVTIGAWLGM
     AAHLQGMEAL ALDMAGLAQK GGAVFSHVQF APAGHTLASS RIPVGEADLM IGGDLVVSAH
     EKTLELLNSQ AFAIVNTDTQ PTADFITQRD WCAPVEQMHA DITGALNNPG QRYTSIRAQW
     LAEKLFGDTV YANALLLGAA WQRGCLPLQL AALRKAIELN GVKVNENLLA FDAGRVAVSK
     PGLLEQMLGK NVAPSAQFES DEDKLSRYQT ELAHYQNEQL AARYAAKVLP LRAMFDSQGL
     KHQWMRLCST YFKLLAFKDE FEVARLHTSP EWQEQTMAQF EPGAKLYFHF APTWLAGHGS
     RPKKIKLGPW IYPLLKILAA SRHLRNTAFD PFRGSLERKN QTLLVTWFET WLELMHNNPS
     MLQHSKQIDH LLDLFNQVKG FGHVRAQSFE QVRFEIQKSV ENKHNLDQHD QSRQQT
//
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