ID A1HPQ5_9FIRM Unreviewed; 367 AA.
AC A1HPQ5;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:EAX48025.1};
GN ORFNames=TcarDRAFT_1903 {ECO:0000313|EMBL:EAX48025.1};
OS Thermosinus carboxydivorans Nor1.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Thermosinus.
OX NCBI_TaxID=401526 {ECO:0000313|EMBL:EAX48025.1, ECO:0000313|Proteomes:UP000005139};
RN [1] {ECO:0000313|EMBL:EAX48025.1, ECO:0000313|Proteomes:UP000005139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nor1 {ECO:0000313|EMBL:EAX48025.1,
RC ECO:0000313|Proteomes:UP000005139};
RG US DOE Joint Genome Institute (JGI-ORNL);
RA Larimer F., Land M., Hauser L.;
RT "Annotation of the draft genome assembly of Thermosinus carboxydivorans
RT Nor1.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAX48025.1, ECO:0000313|Proteomes:UP000005139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nor1 {ECO:0000313|EMBL:EAX48025.1,
RC ECO:0000313|Proteomes:UP000005139};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Richardson P.;
RT "Sequencing of the draft genome and assembly of Thermosinus carboxydivorans
RT Nor1.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007829|PDB:7PD1, ECO:0007829|PDB:7PD2}
RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF 2-367 IN COMPLEX WITH [4FE-4S]
RP CLUSTER.
RX PubMed=35477710; DOI=10.1038/s41467-022-29980-4;
RA Amara P., Saragaglia C., Mouesca J.M., Martin L., Nicolet Y.;
RT "L-tyrosine-bound ThiH structure reveals C-C bond break differences within
RT radical SAM aromatic amino acid lyases.";
RL Nat. Commun. 13:2284-2284(2022).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:EAX48025.1}.
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; AAWL01000005; EAX48025.1; -; Genomic_DNA.
DR RefSeq; WP_007289010.1; NZ_AAWL01000005.1.
DR PDB; 7PD1; X-ray; 1.27 A; A/B=2-367.
DR PDB; 7PD2; X-ray; 1.99 A; A/B=2-367.
DR AlphaFoldDB; A1HPQ5; -.
DR SMR; A1HPQ5; -.
DR eggNOG; COG0502; Bacteria.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000005139; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7PD1, ECO:0007829|PDB:7PD2};
KW 4Fe-4S {ECO:0007829|PDB:7PD1, ECO:0007829|PDB:7PD2};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0007829|PDB:7PD1};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0007829|PDB:7PD1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:7PD1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005139};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 71..292
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0007829|PDB:7PD1, ECO:0007829|PDB:7PD2"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0007829|PDB:7PD1, ECO:0007829|PDB:7PD2"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0007829|PDB:7PD1, ECO:0007829|PDB:7PD2"
SQ SEQUENCE 367 AA; 41786 MW; 5701AD4CD544E5E1 CRC64;
MGTFYDVIED YRHFDFAAYF AKVTDSDVRR ILRQDRLSAL DFLTLLSPQA EAYLEEMAQK
AHRLTVQHFG RTMLLYTPLY LANYCVNQCV YCGFQLKNKL ERKKLTLAEV EQEAQLIAAT
GLKHILILTG ESRQHSPVSY IKDCVNILKK YFSSISIEIY PLTQEEYAEL IGAGVDGLTI
YQEVYNEEVY AEMHPAGPKR NYRFRLEAPE RACQAGMRTV NIGALLGLND WRQEAFFTGL
HADYLQRRFP DVEVSISPPR MRPHLGGFPP RVVVSDQNLV QYVLAFRLFM PRSGITLSTR
ENGRLRDAMV RLGVTKMSAG SCTAVGGRSD QEAVGQFQIS DERTVAEVAA MLYAQGYQPV
YKDWQAL
//
