HEMW_MYCTU
ID HEMW_MYCTU Reviewed; 390 AA.
AC P9WP73; L0TCD5; P71756;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Heme chaperone HemW;
DE AltName: Full=Oxygen-independent coproporphyrinogen-III oxidase-like protein Rv2388c;
GN Name=hemW {ECO:0000250|UniProtKB:P52062}; Synonyms=hemN;
GN OrderedLocusNames=Rv2388c; ORFNames=MTCY253.33;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROTEIN SEQUENCE OF 5-33, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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: Was identified as a high-confidence drug target.
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 -!- SEQUENCE CAUTION:
CC Sequence=CCP45176.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP45176.1; ALT_INIT; Genomic_DNA.
DR PIR; G70681; G70681.
DR RefSeq; NP_216904.1; NC_000962.3.
DR RefSeq; WP_003901389.1; NC_000962.3.
DR AlphaFoldDB; P9WP73; -.
DR SMR; P9WP73; -.
DR STRING; 83332.Rv2388c; -.
DR PaxDb; P9WP73; -.
DR DNASU; 885300; -.
DR GeneID; 885300; -.
DR KEGG; mtu:Rv2388c; -.
DR PATRIC; fig|83332.111.peg.2663; -.
DR TubercuList; Rv2388c; -.
DR eggNOG; COG0635; Bacteria.
DR OMA; HIPWCVR; -.
DR PhylomeDB; P9WP73; -.
DR Proteomes; UP000001584; 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 SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR00539; hemN_rel; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Chaperone; Cytoplasm; Direct protein sequencing; Heme; Iron;
KW Iron-sulfur; Metal-binding; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..390
FT /note="Heme chaperone HemW"
FT /id="PRO_0000109944"
FT DOMAIN 15..254
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 24
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 30
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 34
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 37
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 82
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 83..84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
SQ SEQUENCE 390 AA; 41941 MW; B3125428A47730ED CRC64;
MVFRQAPVEL PGLAPMPGQP FGVYLHVPFC LTRCGYCDFN TYTPAQLGGV SPDRWLLALR
AELELAAAKL DAPTVHTVYV GGGTPSLLGG ERLATLLDMV RDHFVLAPDA EVSTEANPES
TWPEFFATIR AAGYTRVSLG MQSVAPRVLA TLDRVHSPGR AAAAATEAIA EGFTHVNLDL
IYGTPGESDD DLVRSVDAAV QAGVDHVSAY ALVVEHGTAL ARRVRRGELA APDDDVLAHR
YELVDARLSA AGFAWYEVSN WCRPGGECRH NLGYWDGGQW WGAGPGAHGY IGVTRWWNVK
HPNTYAEILA GATLPVAGFE QLGADALHTE DVLLKVRLRQ GLPLARLGAA ERERAEAVLA
DGLLDYHGDR LVLTGRGRLL ADAVVRTLLG
