GenomeNet

Database: UniProt
Entry: D4LWA4_9FIRM
LinkDB: D4LWA4_9FIRM
Original site: D4LWA4_9FIRM 
ID   D4LWA4_9FIRM            Unreviewed;       419 AA.
AC   D4LWA4;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Tyrosine lyase ThiH {ECO:0000313|EMBL:CBL21907.1};
GN   ORFNames=CK5_02840 {ECO:0000313|EMBL:CBL21907.1};
OS   Blautia obeum A2-162.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=657314 {ECO:0000313|EMBL:CBL21907.1, ECO:0000313|Proteomes:UP000008955};
RN   [1] {ECO:0000313|EMBL:CBL21907.1, ECO:0000313|Proteomes:UP000008955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2-162 {ECO:0000313|EMBL:CBL21907.1,
RC   ECO:0000313|Proteomes:UP000008955};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Ruminococcus obeum A2-162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL21907.1, ECO:0000313|Proteomes:UP000008955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A2-162 {ECO:0000313|EMBL:CBL21907.1,
RC   ECO:0000313|Proteomes:UP000008955};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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; FP929054; CBL21907.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4LWA4; -.
DR   KEGG; rob:CK5_02840; -.
DR   PATRIC; fig|657314.3.peg.993; -.
DR   HOGENOM; CLU_046249_1_0_9; -.
DR   Proteomes; UP000008955; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01335; Radical_SAM; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR010722; BATS_dom.
DR   InterPro; IPR007197; rSAM.
DR   InterPro; IPR012726; ThiH.
DR   InterPro; IPR034428; ThiH/NoCL/HydG-like.
DR   NCBIfam; TIGR02351; thiH; 1.
DR   PANTHER; PTHR43583; 2-IMINOACETATE SYNTHASE; 1.
DR   PANTHER; PTHR43583:SF1; 2-IMINOACETATE SYNTHASE; 1.
DR   Pfam; PF06968; BATS; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00301; 2-iminoacetate_synthase_(ThiH); 1.
DR   SFLD; SFLDG01081; cleavage_of_the_Ca-Cb_bond_in; 1.
DR   SMART; SM00876; BATS; 1.
DR   SUPFAM; SSF102114; Radical SAM enzymes; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000313|EMBL:CBL21907.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          300..411
FT                   /note="Biotin and thiamin synthesis-associated"
FT                   /evidence="ECO:0000259|SMART:SM00876"
SQ   SEQUENCE   419 AA;  48253 MW;  221CB73FFD0BC3C1 CRC64;
     MNEENQVYFI DSDKLPPAAL KRKHRLEQDP SFRTNHMEYM EGMQVIESDI KDKVLHAMDT
     YDYDAYTAGD VERALSHESC SIEDFKALLS PAAAPYLEQM ARKAEELTKN HFGNTVYIFT
     PLYIANYCQN YCIYCGFNCY NNIRRKKLTF EEIEHEMQVI AKTGMEEILM LTGESRAYSD
     VKYIGEAVKI ARKYFKNIGI EIYPVNVDEY QYLHECGVDY VTVFQETYNT DKYETLHLMG
     HKRVWPYRFD AQERALMGGM RGAGFSALLG LDDFRKDALA TALHVYYINR KYPHAELSLS
     CPRLRPIVNN DRINPRDVGE KELCQVLCAY RIFLPFAGIT VSSRESATFR NGIAKICATK
     VSAGVSTGIG DHEEKYEGKE DDNVGDEQFE INDDRSFGKM YEDMEQGGLQ PVLNDYIYV
//
DBGET integrated database retrieval system