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LOCUS WP_001096518 378 aa linear BCT 04-JUN-2024 ACCESSION WP_001096518 VERSION WP_001096518.1 KEYWORDS RefSeq. SOURCE Salmonella ORGANISM Salmonella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 378) AUTHORS Haskamp,V., Karrie,S., Mingers,T., Barthels,S., Alberge,F., Magalon,A., Muller,K., Bill,E., Lubitz,W., Kleeberg,K., Schweyen,P., Broring,M., Jahn,M. and Jahn,D. TITLE The radical SAM protein HemW is a heme chaperone JOURNAL J Biol Chem 293 (7), 2558-2572 (2018) PUBMED 29282292 REFERENCE 2 (residues 1 to 378) AUTHORS Abicht,H.K., Martinez,J., Layer,G., Jahn,D. and Solioz,M. TITLE Lactococcus lactis HemW (HemN) is a haem-binding protein with a putative role in haem trafficking JOURNAL Biochem J 442 (2), 335-343 (2012) PUBMED 22142238 REFERENCE 3 (residues 1 to 378) AUTHORS Homuth,G., Heinemann,M., Zuber,U. and Schumann,W. TITLE The genes of lepA and hemN form a bicistronic operon in Bacillus subtilis JOURNAL Microbiology (Reading) 142 (Pt 7), 1641-1649 (1996) PUBMED 8757728 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR00539.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..378 /organism="Salmonella" /db_xref="taxon:590" gene 1..378 /gene="hemW" Protein 1..378 /product="radical SAM family heme chaperone HemW" /GO_component="GO:0005737 - cytoplasm [Evidence IEA]" /GO_function="GO:0051539 - 4 iron, 4 sulfur cluster binding [Evidence IEA]" /GO_function="GO:0051989 - coproporphyrinogen dehydrogenase activity [Evidence IEA]" /GO_process="GO:0006779 - porphyrin-containing compound biosynthetic process [Evidence IEA]" /calculated_mol_wt=42643 Region 1..378 /region_name="HemN" /note="Coproporphyrinogen-III oxidase HemN (oxygen-independent) or related Fe-S oxidoreductase [Coenzyme transport and metabolism]; COG0635" /db_xref="CDD:440400" ORIGIN 1 maklpplsly ihipwcvqkc pycdfnshal kgevphddyv qhllndldad vawaqgrevk 61 tifigggtps llsgpamqtl ldgvrarlnl aadaeitmea npgtveadrf idyqragvnr 121 isigvqsfse pklkrlgrih gpqeakraar langlglrsf nldlmhglpd qtleealndl 181 rqaialnpph lswyqltiep ntlfgsrppv lpdddalwdi feqghqllta agyqqyetsa 241 yakpgyqcqh nlnywrfgdy lgigcgahgk vtfpdgrilr ttktrhprgy mqgrylesqr 301 dvsdddkpfe ffmnrfrlle rapraefvdy tglteavirq pideaiaqgy lteceqywqi 361 trhgklflns llelflae