ID Q0P9K8_CAMJE Unreviewed; 381 AA.
AC Q0P9K8;
DT 19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 19-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:CAL35162.1};
GN Name=thiH {ECO:0000313|EMBL:CAL35162.1};
GN OrderedLocusNames=Cj1044c {ECO:0000313|EMBL:CAL35162.1};
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL35162.1, ECO:0000313|Proteomes:UP000000799};
RN [1] {ECO:0000313|EMBL:CAL35162.1, ECO:0000313|Proteomes:UP000000799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799};
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D.,
RA Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K.,
RA Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A.,
RA Rutherford K.M., VanVliet A., Whitehead S., Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL35162.1; -; Genomic_DNA.
DR PIR; A81307; A81307.
DR RefSeq; WP_002857955.1; NZ_SZUC01000001.1.
DR RefSeq; YP_002344439.1; NC_002163.1.
DR AlphaFoldDB; Q0P9K8; -.
DR IntAct; Q0P9K8; 5.
DR STRING; 192222.Cj1044c; -.
DR PaxDb; 192222-Cj1044c; -.
DR EnsemblBacteria; CAL35162; CAL35162; Cj1044c.
DR GeneID; 905336; -.
DR KEGG; cje:Cj1044c; -.
DR PATRIC; fig|192222.6.peg.1026; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_1_0_7; -.
DR OrthoDB; 3320990at2; -.
DR Proteomes; UP000000799; Chromosome.
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.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000000799};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 268..372
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 381 AA; 43070 MW; DFB9C2F8CACC928C CRC64;
MQDYMQHLPH MQEIKSEILN KVLTQVQSYD ESQFSAKDVK NALNQTHLSI EHLKALLSSA
AEDFIEELAF KSAKVKQKYF GNSISLFTPL YLSNYCNSKC VYCGFQKGNK IARAKLNEAE
IHEEMQAIAK SGLEEILMLT GEGREFASVE YIANACKIAR EYFKVVGVEI YPMNEDEYKI
LHEKGCDYVT VFQETYNPLK YSKIHLAGEK RIFPYRFNAQ ERALKAGMRG VAFAALLGID
DFRKDALATA LHAHFLQQAY SHAEISISVP RLRPIINNAK IHPKDVSEKR LLQVLCAYRL
FLPFAGITIS SRERIGFRDE VIKLGATKMS AGVSVGIGEH KGEKKGDEQF EISDDRSVDE
ILAMLKRSNL QAVMSDSIYV G
//
