HEMW_BUCAP
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 03-AUG-2022, entry version 107.
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; Proteobacteria; 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}.
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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 EnsemblBacteria; AAM68073; AAM68073; BUsg_532.
DR KEGG; bas:BUsg_532; -.
DR eggNOG; COG0635; Bacteria.
DR HOGENOM; CLU_027579_2_1_6; -.
DR OMA; HIPWCVR; -.
DR OrthoDB; 1130951at2; -.
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 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 SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00539; hemN_rel; 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
