(data stored in SCRATCH zone)

SWISSPROT: A0KFF1_AERHH

ID   A0KFF1_AERHH            Unreviewed;       423 AA.
AC   A0KFF1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   SubName: Full=Thiazole biosynthesis protein ThiH {ECO:0000313|EMBL:ABK39165.1};
GN   Name=thiH {ECO:0000313|EMBL:ABK39165.1};
GN   OrderedLocusNames=AHA_0444 {ECO:0000313|EMBL:ABK39165.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39165.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39165.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|SAAS:SAAS00610634};
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DR   EMBL; CP000462; ABK39165.1; -; Genomic_DNA.
DR   RefSeq; WP_011704418.1; NC_008570.1.
DR   RefSeq; YP_854973.1; NC_008570.1.
DR   STRING; 380703.AHA_0444; -.
DR   EnsemblBacteria; ABK39165; ABK39165; AHA_0444.
DR   GeneID; 4490407; -.
DR   KEGG; aha:AHA_0444; -.
DR   PATRIC; fig|380703.7.peg.434; -.
DR   eggNOG; ENOG4105D41; Bacteria.
DR   eggNOG; COG1060; LUCA.
DR   HOGENOM; HOG000270732; -.
DR   KO; K03150; -.
DR   OMA; LICAYRL; -.
DR   BioCyc; AHYD380703:G1G7B-445-MONOMER; -.
DR   Proteomes; UP000000756; 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   Gene3D; 3.20.20.70; -; 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   PANTHER; PTHR43583; PTHR43583; 1.
DR   PANTHER; PTHR43583:SF1; PTHR43583:SF1; 1.
DR   Pfam; PF06968; BATS; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   SFLD; SFLDF00301; 2-iminoacetate_synthase_(ThiH); 1.
DR   SFLD; SFLDS00029; Radical_SAM; 1.
DR   SMART; SM00876; BATS; 1.
DR   TIGRFAMs; TIGR02351; thiH; 1.
PE   4: Predicted;
DR   PRODOM; A0KFF1.
DR   SWISS-2DPAGE; A0KFF1.
KW   4Fe-4S {ECO:0000256|SAAS:SAAS00448030};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
KW   Iron {ECO:0000256|SAAS:SAAS00448063};
KW   Iron-sulfur {ECO:0000256|SAAS:SAAS00448067};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00448059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00448054}.
FT   DOMAIN      308    412       BATS. {ECO:0000259|SMART:SM00876}.
FT   COILED      150    170       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   423 AA;  47042 MW;  DD1645F29B814557 CRC64;
     MSSFSVSPEA DVFSPPLPLG EGLGVRAEAD SVLEGGEPCT PPPPKGEAGR GLDFANRWQE
     LEWDDIGMQI RAKTAADVAR ALSAPRRTLA DFMALISPAA EAYLPQMAAE AERLTRQRFG
     NTIGFYVPLY LSNLCANDCT YCGFSMSNRL KRKTLNAEEI ERECLAIKAR GFDSVLLVTG
     EHEHKVGLAY FREVMPIIRR HFSTVGMEVQ PLSQDEYAEL KSLGLDSVMV YQETYHAPTY
     ARHHLRGNKR EIAWRLATPD RLGRAGIDKI GLGALIGLSS DWRADSYFVA EHLAWLERHH
     WQSRYSLSFP RLRPCTGGLE PAVVMSDRQL AQLICAWRLF SPTLDLSLST RESATFRNGA
     VRLGITQMSA ESRTQPGGYA EGDAEELEQF AIHDDRPVGE VAAAVRQAGL QPVFKDWEPF
     LGR
//

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