ID A0A809GW50_MYCCH Unreviewed; 391 AA. AC A0A809GW50; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, entry version 2. DE RecName: Full=Heme chaperone HemW {ECO:0000256|ARBA:ARBA00017228, ECO:0000256|RuleBase:RU364116}; GN ORFNames=DYE20_08620 {ECO:0000313|EMBL:AYM41600.1}; OS [Mycobacterium] chelonae subsp. gwanakae. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacteroides. OX NCBI_TaxID=2480908 {ECO:0000313|EMBL:AYM41600.1, ECO:0000313|Proteomes:UP000265679}; RN [1] {ECO:0000313|EMBL:AYM41600.1, ECO:0000313|Proteomes:UP000265679} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MOTT36W {ECO:0000313|EMBL:AYM41600.1, RC ECO:0000313|Proteomes:UP000265679}; RA Kim B.-J., Kim B.-R., Jeong J., Lim J.-H., Park S.H., Lee S.-H., Kim C.K., RA Kook Y.-H., Kim B.-J.; RT "Mycobacterium chelonae Genome sequencing and assembly."; RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Probably acts as a heme chaperone, transferring heme to an CC unknown acceptor. Binds one molecule of heme per monomer, possibly CC covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000256|RuleBase:RU364116}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364116}. CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase CC family. HemW subfamily. {ECO:0000256|ARBA:ARBA00006100}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP031516; AYM41600.1; -; Genomic_DNA. DR RefSeq; WP_070921668.1; NZ_CP031516.1. DR Proteomes; UP000265679; Chromosome. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR004559; HemW-like. DR InterPro; IPR007197; rSAM. DR PANTHER; PTHR13932; PTHR13932; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00539; hemN_rel; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|RuleBase:RU364116}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU364116}; KW Cytoplasm {ECO:0000256|RuleBase:RU364116}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU364116}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364116}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364116}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU364116}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, KW ECO:0000256|RuleBase:RU364116}. FT DOMAIN 14..255 FT /note="Radical SAM core" FT /evidence="ECO:0000259|PROSITE:PS51918" SQ SEQUENCE 391 AA; 41425 MW; CC9A16B158A2BE4E CRC64; MRPETIATLP PLVPAPGRPF GIYVHVPFCA TRCGYCDFNT YTADELGDGT SPAGWLEALR AELDLAARTL DGKPPVETVF VGGGTPSLLG GSGLAEVLDA IGAHFTLAPG AEVTTEANPE STSPAFFETI RAAGYTRVSL GMQSAAPHVL ATLDRVHAPG RAVAAAREAR AAGLEHVNLD LIYGTPGETD DDLRRSIDAV LDAGVDHVSA YALVVEEGTA LARRVRRGEL PNPDEDALAD RYQLLDTALS QAGLSWYEVS NWARPGGQCR HNLGYWAGGD WWGAGPGAHG HVNGVRWWNV KHPNTYAKQL GAGQLPVGGH EILSPAERHT EDVLLAVRLN TGIALADLTV EERGRVPAVV SGGLARLVDD RLVLTDQGRL LADGVVRTIL D //