ID A9L3J2_SHEB9 Unreviewed; 371 AA.
AC A9L3J2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:ABX49602.1};
GN OrderedLocusNames=Sbal195_2434 {ECO:0000313|EMBL:ABX49602.1};
OS Shewanella baltica (strain OS195).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX49602.1, ECO:0000313|Proteomes:UP000000770};
RN [1] {ECO:0000313|EMBL:ABX49602.1, ECO:0000313|Proteomes:UP000000770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS195 {ECO:0000313|EMBL:ABX49602.1,
RC ECO:0000313|Proteomes:UP000000770};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS195.";
RL Submitted (NOV-2007) 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; CP000891; ABX49602.1; -; Genomic_DNA.
DR RefSeq; WP_006086791.1; NC_009997.1.
DR AlphaFoldDB; A9L3J2; -.
DR GeneID; 11774796; -.
DR KEGG; sbn:Sbal195_2434; -.
DR HOGENOM; CLU_046249_1_0_6; -.
DR Proteomes; UP000000770; 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 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; 41949 MW; 6A4CEAA71E1C2184 CRC64;
MSFVAEFANI PRDKLLLDLY SCTAQDVERA LVSPAGDLRS LLALLSPAAE PYIETMAQHS
AALTRQRFGA NLGMYLPLYV SNLCANECDY CGFSMSNKLK RKTLNEQELM AEMAIIKDRG
FDSILLVSGE HETKVGIDYF KQMLPLVKQQ FSHLAMEVQP MSEDHYCQLV ALGLDAVMIY
QETYQPETYA RHHSRGKKMD FAYRLATPDR VAAAGVDKIG LGVLLGLDDW RLDALMMGYH
LDYLERRYWR TRFSISLPRL RPCTGGITPK VMLSDLGLVQ MICAFRLFNQ QLNISMSTRE
SPELRDNLLP LGITQISAGS STQPGGYQAP DSQLDQFEIS DDRSVEQVIE QMQRQGFNPV
FKDWEANWIT G
//
