ID A0A0E3GRX2_CLOSL Unreviewed; 327 AA.
AC A0A0E3GRX2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thiamine biosynthesis protein {ECO:0000313|EMBL:AKA71066.1};
GN ORFNames=CSCA_3941 {ECO:0000313|EMBL:AKA71066.1};
OS Clostridium scatologenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1548 {ECO:0000313|EMBL:AKA71066.1, ECO:0000313|Proteomes:UP000033115};
RN [1] {ECO:0000313|Proteomes:UP000033115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25775 {ECO:0000313|Proteomes:UP000033115};
RA Xie J., Zhu Z., Guo T., Song T.;
RT "Complete Genome Sequence of the Malodorant-Producing Specialist,
RT Clostridium scatologenes ATCC 25775.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKA71066.1, ECO:0000313|Proteomes:UP000033115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25775 {ECO:0000313|EMBL:AKA71066.1,
RC ECO:0000313|Proteomes:UP000033115};
RX PubMed=26210291; DOI=10.1016/j.jbiotec.2015.07.013;
RA Zhu Z., Guo T., Zheng H., Song T., Ouyang P., Xie J.;
RT "Complete genome sequence of a malodorant-producing acetogen, Clostridium
RT scatologenes ATCC 25775(T).";
RL J. Biotechnol. 212:19-20(2015).
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; CP009933; AKA71066.1; -; Genomic_DNA.
DR RefSeq; WP_029159238.1; NZ_CP009933.1.
DR AlphaFoldDB; A0A0E3GRX2; -.
DR STRING; 1548.CSCA_3941; -.
DR KEGG; csq:CSCA_3941; -.
DR HOGENOM; CLU_053822_0_0_9; -.
DR Proteomes; UP000033115; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:InterPro.
DR CDD; cd01712; ThiI; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR020536; ThiI_AANH.
DR PANTHER; PTHR11933:SF6; THIL AANH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11933; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE; 1.
DR Pfam; PF18297; NFACT-R_2; 1.
DR Pfam; PF02568; ThiI; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 3..141
FT /note="Thil AANH"
FT /evidence="ECO:0000259|Pfam:PF02568"
SQ SEQUENCE 327 AA; 37078 MW; CE0DCB213E2BEC7F CRC64;
MTKALAMMSG GLDSVLAAKL IKDQGIEVVG ICFKSYFFGP DNAIRMAKQI DVPLEVVDFS
EEHFEMVKNP KHGYGKNINP CIDCHAMMMN YSGKMLEKYE ADFIITGEVL NQRPMSQNKS
SLDVVKRESG FSDKILRPLC AKNLAPTKME LEGLVDREKL MDISGRSRKV QMELAEKWGI
KDYPSPAGGC KLTEPNYSKR LKDILDKKED VIARDLGVLK YGRHFRISEK AKIISTRTAE
EAQEIKQYLT TKDMIFLAND FNGSMVMIIG EATEEDIEFA AKVTGRYCKG KNEEKIEIKY
GYYKQPLDKF IEVKAATEEE LSKYILP
//