ID HEMW_BUCAP Reviewed; 376 AA. AC Q8K928; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=Heme chaperone HemW; DE AltName: Full=Oxygen-independent coproporphyrinogen-III oxidase-like protein BUsg_532; GN Name=hemW {ECO:0000250|UniProtKB:P52062}; OrderedLocusNames=BUsg_532; OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=198804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sg; RX PubMed=12089438; DOI=10.1126/science.1071278; RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; RT "50 million years of genomic stasis in endosymbiotic bacteria."; RL Science 296:2376-2379(2002). 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 (By similarity). Binds 1 [4Fe-4S] cluster. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine (By similarity). {ECO:0000250|UniProtKB:P32131, CC ECO:0000250|UniProtKB:P52062}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01266}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CGF7}. CC -!- MISCELLANEOUS: Might carry two S-adenosyl-L-methionine binding sites CC with only one binding to the iron-sulfur cluster. CC {ECO:0000250|UniProtKB:P32131}. CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase CC family. HemW subfamily. {ECO:0000305}. 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; AE013218; AAM68073.1; -; Genomic_DNA. DR RefSeq; WP_011054039.1; NC_004061.1. DR AlphaFoldDB; Q8K928; -. DR SMR; Q8K928; -. DR STRING; 198804.BUsg_532; -. DR GeneID; 75258580; -. DR KEGG; bas:BUsg_532; -. DR eggNOG; COG0635; Bacteria. DR HOGENOM; CLU_027579_2_1_6; -. DR Proteomes; UP000000416; Chromosome. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; ISS:UniProtKB. DR CDD; cd01335; Radical_SAM; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR034505; Coproporphyrinogen-III_oxidase. DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM. DR InterPro; IPR010723; HemN_C. DR InterPro; IPR004559; HemW-like. DR InterPro; IPR007197; rSAM. DR NCBIfam; TIGR00539; hemN_rel; 1. DR PANTHER; PTHR13932; COPROPORPHYRINIGEN III OXIDASE; 1. DR PANTHER; PTHR13932:SF5; RADICAL S-ADENOSYL METHIONINE DOMAIN-CONTAINING PROTEIN 1, MITOCHONDRIAL; 1. DR Pfam; PF06969; HemN_C; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SFLD; SFLDG01065; anaerobic_coproporphyrinogen-I; 1. DR SFLD; SFLDG01082; B12-binding_domain_containing; 1. DR SFLD; SFLDF00562; HemN-like__clustered_with_heat; 1. DR SFLD; SFLDF00288; HemN-like__clustered_with_nucl; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF102114; Radical SAM enzymes; 1. DR PROSITE; PS51918; RADICAL_SAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Chaperone; Cytoplasm; Heme; Iron; Iron-sulfur; Metal-binding; KW S-adenosyl-L-methionine. FT CHAIN 1..376 FT /note="Heme chaperone HemW" FT /id="PRO_0000109959" FT DOMAIN 1..236 FT /note="Radical SAM core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266" FT BINDING 10 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 16 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 20 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 23 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 66 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 67..68 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 99 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 126 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 138 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P32131" FT BINDING 162 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P32131" SQ SEQUENCE 376 AA; 44581 MW; 4808E9524404C0F6 CRC64; MFKLPPISLY IHIPWCIKKC GYCDFYSYVN KSFIPEKEYI DHLLKDLEKD LSLIKEREIN SIFIGGGTPS LLKSSSIKKM MREIKKRINI SNTAEITIEA NPTTLEYKRF FNYKKSGINR FSIGVQTFNS DLLKKIERTY NKREAILAVE EIKKINKNFN LDIMYGLPNQ SLKDVLLDLQ YAVKYNPTHI SWYQLTLEPN TPFYVKKLNL PNENNIFKML VEGEKFLKQS GYKKYEISSY AKLNYECQHN LNYWNFGDYI GIGCSAHGKI TQINGDIIRT IKNKNINDFM NGKYLKHKNF VLKKDKPFEY FMNIFRLYKP VLKRQFEERT NINQNYIKEK IKKAIEKGYL KNKIDFWDTT KKGKMFLNSL LKIFLD //