ID E0SGG4_DICD3 Unreviewed; 417 AA.
AC E0SGG4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Thiamin biosynthesis ThiGH complex subunit {ECO:0000313|EMBL:ADM96450.1};
DE EC=2.8.1.6 {ECO:0000313|EMBL:ADM96450.1};
GN Name=thiH {ECO:0000313|EMBL:ADM96450.1};
GN OrderedLocusNames=Dda3937_00230 {ECO:0000313|EMBL:ADM96450.1};
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADM96450.1, ECO:0000313|Proteomes:UP000006859};
RN [1] {ECO:0000313|EMBL:ADM96450.1, ECO:0000313|Proteomes:UP000006859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937 {ECO:0000313|EMBL:ADM96450.1,
RC ECO:0000313|Proteomes:UP000006859};
RX PubMed=21217001; DOI=10.1128/JB.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP002038; ADM96450.1; -; Genomic_DNA.
DR AlphaFoldDB; E0SGG4; -.
DR STRING; 198628.Dda3937_00230; -.
DR KEGG; ddd:Dda3937_00230; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_1_0_6; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-EC.
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 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:UP000006859};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000313|EMBL:ADM96450.1}.
FT DOMAIN 112..342
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 47623 MW; 1B7F0C52735D458C CRC64;
MDSQLIDSQS IDNQTIDGQT IDRQTMDSQT MDSQTIDGKH QPPSFERHWQ QLEWHDLTLR
INSKTDADVE RALCADRLTR EDMMALLSPA AGRWLEPLAQ RAQQLTRQRF GNTVSFYVPL
YLSNLCANDC TYCGFSMSNH LKRKTLDEQE ILRECEAIKA LGFDHLLLVT GEHQRKVGMD
YFRQMLPLIR PQFSSLMMEV QPLSQAEYAE LKTLGLDGVM VYQETYHPAT YARHHLRGHK
QDFAWRLATP DRLGRAGIDK IGLGALIGLS DSWRTDCYMV AEHLLYLQQT YWQSRYSVSF
PRLRPCAGGI EPASLMDEAQ LMQVICAFRL LAPDVELSLS TRESPFFRDH MIPIAINNVS
AFSKTQPGGY ADDHPELEQF TPHDNRRPQA VADALTRAGL QPVWKDWDGY LGRPVTG
//
