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LOCUS WP_003114885 384 aa linear BCT 04-JUN-2024 ACCESSION WP_003114885 VERSION WP_003114885.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 384) 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 384) 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 384) 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..384 /organism="Pseudomonas" /db_xref="taxon:286" gene 1..384 /gene="hemW" Protein 1..384 /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=42429 Region 8..384 /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 mtqatpfqlp plalyvhipw cvrkcpycdf nshaagpelp eeayvdalla dleqdlrhvh 61 grrlgsiffg ggtpslfsak algrllegve rrvgfadgie itleanpgtf eqvkfadyrr 121 lginrlsigv qsfqadklqa lgrihdgaea vraadmarqa gfdnfnldlm hglpgqsldd 181 aladlrqala lapthlswyq ltmepntvfw sqppelpedd ilwdiqeagq alldehgyrq 241 yetsayardg lrarhnlnyw sfgdflgiga gahaklsapd grivrtwktr lpkdylnpqk 301 afqagerple aadlpfefmm nvlrlvdgvp aalypqrtgq plaaiadaca aardagllad 361 dpqhlrpser gqlflndllq hflp