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Database: UniProt
Entry: A6EM46_9BACT
LinkDB: A6EM46_9BACT
Original site: A6EM46_9BACT 
ID   A6EM46_9BACT            Unreviewed;       369 AA.
AC   A6EM46;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Thiamine biosynthesis protein {ECO:0000313|EMBL:EDM45646.1};
GN   ORFNames=SCB49_07552 {ECO:0000313|EMBL:EDM45646.1};
OS   unidentified eubacterium SCB49.
OC   Bacteria; Bacteroidota; environmental samples.
OX   NCBI_TaxID=50743 {ECO:0000313|EMBL:EDM45646.1, ECO:0000313|Proteomes:UP000003659};
RN   [1] {ECO:0000313|EMBL:EDM45646.1, ECO:0000313|Proteomes:UP000003659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCB49 {ECO:0000313|EMBL:EDM45646.1,
RC   ECO:0000313|Proteomes:UP000003659};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-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   -!- 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:EDM45646.1}.
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DR   EMBL; ABCO01000001; EDM45646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6EM46; -.
DR   STRING; 50743.SCB49_07552; -.
DR   Proteomes; UP000003659; 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; SFLDG01060; BATS_domain_containing; 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:UP000003659};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT   DOMAIN          70..314
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000259|PROSITE:PS51918"
SQ   SEQUENCE   369 AA;  42345 MW;  17479476A1A4F1CD CRC64;
     MSFSEQIKQI KWDTVKASIY NKTANDVAVA LSKTKRDLED FKALISPAAQ PYLEQMAQLS
     NQLTQKRFGK TIQMYIPMYL SNECQNICTY CGFSLNVDIT RKTLTDAEII TEAKIIKNLG
     YDHILLVTGE ANKTVGVDYF VNAIRLLKPF FAHIAIEVQP LDQEEYETLI DEGINTVLVY
     QETYKKDAYK KHHPKGKKSN FEYRLKTHDR LGKAGIYKMG LGVLFGLEDW RVDTYFCASH
     LSYLEKTYWK SKYSISFPRL RPCAGGIELK SVMSDKELVQ LICAYRIFNE EVELSISTRE
     SERFRDHIIK LGITSASADS KTDPGGYANP NTNLEQFEID DTRPTKTFIE VIKNQGYDPV
     FKDWDSSLQ
//
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