ID D4ZKY8_SHEVD Unreviewed; 371 AA.
AC D4ZKY8;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Thiazole biosynthesis protein thiH {ECO:0000313|EMBL:BAJ02337.1};
GN Name=thiH {ECO:0000313|EMBL:BAJ02337.1};
GN OrderedLocusNames=SVI_2366 {ECO:0000313|EMBL:BAJ02337.1};
OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ02337.1, ECO:0000313|Proteomes:UP000002350};
RN [1] {ECO:0000313|Proteomes:UP000002350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC {ECO:0000313|Proteomes:UP000002350};
RX PubMed=20458400; DOI=10.1039/c000396d;
RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA Nakasone K., Mori H.;
RT "Complete genome sequence and comparative analysis of Shewanella violacea,
RT a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL Mol. Biosyst. 6:1216-1226(2010).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; AP011177; BAJ02337.1; -; Genomic_DNA.
DR RefSeq; WP_013051641.1; NC_014012.1.
DR AlphaFoldDB; D4ZKY8; -.
DR STRING; 637905.SVI_2366; -.
DR KEGG; svo:SVI_2366; -.
DR eggNOG; COG0502; Bacteria.
DR HOGENOM; CLU_046249_1_0_6; -.
DR OrthoDB; 9801120at2; -.
DR Proteomes; UP000002350; 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:UP000002350};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 256..359
FT /note="Biotin and thiamin synthesis-associated"
FT /evidence="ECO:0000259|SMART:SM00876"
SQ SEQUENCE 371 AA; 41632 MW; 6E28927AD9488A3A CRC64;
MSFLSYLQGI SREKLKLALY SATSLDVERA LNSAEGDLNS LLALLSPAAE PYIEQMAQQS
VRLTRQRFGA NIGMFLPLYL SNLCANECDY CGFSMSNKLK RKTLNSPELE AEMAVIKQLG
YDSILLVSGE HETKVGIDYF KQVLPQVKKQ FSYLAMEVQP LAEHEYSELV GLGLDAVMVY
QETYNPQTYA KHHTRGKKKD FAYRLDTPER VAKAGVDKIG LGVLLGLDDW RLDALLLGHH
LAYLESKYWR SRYSVSLPRL RPCTGGISPK VELTDKGLVQ LICAFRLFNQ QLDISLSTRE
SPEFRDNLFS LGITNVSAGS STQPGGYVKP DTELDQFEIS DDRTPAQVSH AMKQRGLNPV
WKDWESAWVA G
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