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LOCUS WP_002892189 320 aa linear BCT 24-OCT-2022 ACCESSION WP_002892189 VERSION WP_002892189.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 320) AUTHORS Burden,A.E., Wu,C., Dailey,T.A., Busch,J.L., Dhawan,I.K., Rose,J.P., Wang,B. and Dailey,H.A. TITLE Human ferrochelatase: crystallization, characterization of the [2Fe-2S] cluster and determination that the enzyme is a homodimer JOURNAL Biochim Biophys Acta 1435 (1-2), 191-197 (1999) PUBMED 10561552 REFERENCE 2 (residues 1 to 320) AUTHORS Miyamoto,K., Kanaya,S., Morikawa,K. and Inokuchi,H. TITLE Overproduction, purification, and characterization of ferrochelatase from Escherichia coli JOURNAL J Biochem 115 (3), 545-551 (1994) PUBMED 8056770 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 :: TIGR00109.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..320 /organism="Klebsiella" /db_xref="taxon:570" gene 1..320 /gene="hemH" Protein 1..320 /product="ferrochelatase" /EC_number="4.98.1.1" /GO_function="GO:0004325 - ferrochelatase activity [Evidence IEA]" /GO_process="GO:0006779 - porphyrin-containing compound biosynthetic process [Evidence IEA]" /calculated_mol_wt=35656 Region 5..315 /region_name="HemH" /note="Protoheme ferro-lyase (ferrochelatase) [Coenzyme transport and metabolism]; COG0276" /db_xref="CDD:440045" ORIGIN 1 mhqtktgill anlgtpdapt pgavkrylrq flsdkrvvdt srllwwpllr gvilpirspr 61 vaklyqsvwm eegsplmvys rrqqqalaar lpdtpvalgm sygspslasa vddllaqgve 121 hivvlplypq yscstvaavw delarilakk raipgisfir dyaehpdyih alaasvrasf 181 avhgepdlll lsyhgipqry anqgddypqr crdttrelvs alglppervm mtfqsrfgre 241 pwltpytdet lkmlgekgtk hiqvlcpgfa adcletleei avqnreifle aggkqyeyip 301 alnadaahie mmvnltapyr