GenomeNet

Database: UniProt
Entry: A0A0Q5TK09_9BACT
LinkDB: A0A0Q5TK09_9BACT
Original site: A0A0Q5TK09_9BACT 
ID   A0A0Q5TK09_9BACT        Unreviewed;       349 AA.
AC   A0A0Q5TK09;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Thiamine biosynthesis protein ThiF {ECO:0000313|EMBL:KQS31079.1};
GN   ORFNames=ASG33_12035 {ECO:0000313|EMBL:KQS31079.1};
OS   Dyadobacter sp. Leaf189.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=1736295 {ECO:0000313|EMBL:KQS31079.1, ECO:0000313|Proteomes:UP000051810};
RN   [1] {ECO:0000313|EMBL:KQS31079.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf189 {ECO:0000313|EMBL:KQS31079.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS31079.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf189 {ECO:0000313|EMBL:KQS31079.1};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQS31079.1}.
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; LMPS01000004; KQS31079.1; -; Genomic_DNA.
DR   RefSeq; WP_056285008.1; NZ_LMPS01000004.1.
DR   AlphaFoldDB; A0A0Q5TK09; -.
DR   STRING; 1736295.ASG33_12035; -.
DR   OrthoDB; 9804286at2; -.
DR   Proteomes; UP000051810; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   CDD; cd00158; RHOD; 1.
DR   CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR   PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051810};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          274..339
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   349 AA;  38504 MW;  D3E68E8FE4436060 CRC64;
     MLKLEIQERK RYSRQILLPE VGLEGQEKLK SARVLVVGAG GLGCPVLQYL TAAGVGEIGI
     IDHDHVEVTN LHRQILYSEA DLGKKKAVTA AEKLSILNGF VKFTPYPVQL TSENAAEIIS
     GYDLVIDGSD NFETRYLVND TCIKLNKTWV FGSILRFEGQ VSVFNHHNGP TYRCLFPDAE
     EGDNCAEAGV IGILPGIIGT YMANEAIKVI CEVGQVLSGR LLLINALTNA TSTFEFSRNI
     PVQDSPVTEP APSPKPVDAR EMSLEEFERI QDAAPEQVQF IDVREDYEFE ADNFGGTNIP
     LSEIPDFLTT FPDDKTVVFY CQSGIRSRQA AKLLLKSGFL GDARWAANW
//
DBGET integrated database retrieval system