CHUW_ECO57
ID CHUW_ECO57 Reviewed; 445 AA.
AC A0A384LP51;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Anaerobilin synthase {ECO:0000305};
DE EC=2.1.1.342 {ECO:0000269|PubMed:27791000};
GN Name=chuW {ECO:0000303|PubMed:27791000};
GN OrderedLocusNames=Z4914 {ECO:0000312|EMBL:AAG58644.1};
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=27791000; DOI=10.1073/pnas.1603209113;
RA LaMattina J.W., Nix D.B., Lanzilotta W.N.;
RT "Radical new paradigm for heme degradation in Escherichia coli O157:H7.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:12138-12143(2016).
CC -!- FUNCTION: Involved in heme degradation and iron utilization under
CC anaerobic conditions. Catalyzes a radical-mediated mechanism
CC facilitating iron liberation and the production of the tetrapyrrole
CC product anaerobilin. Can use heme, mesoheme and deuteroheme as
CC substrates. {ECO:0000269|PubMed:27791000}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=heme b + 2 reduced [flavodoxin] + 2 S-adenosyl-L-methionine =
CC 5'-deoxyadenosine + anaerobilin + Fe(2+) + L-methionine + 2 oxidized
CC [flavodoxin] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15429,
CC Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:10623, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:57618, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58210, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:60344, ChEBI:CHEBI:136517; EC=2.1.1.342;
CC Evidence={ECO:0000269|PubMed:27791000};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:27791000};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:P32131};
CC -!- ACTIVITY REGULATION: Inhibited by exposure to molecular oxygen.
CC {ECO:0000269|PubMed:27791000}.
CC -!- SIMILARITY: Belongs to the anaerobic coproporphyrinogen-III oxidase
CC family. ChuW/HutW subfamily. {ECO:0000305}.
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DR EMBL; AE005174; AAG58644.1; -; Genomic_DNA.
DR PIR; G91176; G91176.
DR PIR; H86022; H86022.
DR RefSeq; WP_000993317.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; A0A384LP51; -.
DR SMR; A0A384LP51; -.
DR STRING; 155864.EDL933_4753; -.
DR EnsemblBacteria; AAG58644; AAG58644; Z4914.
DR KEGG; ece:Z4914; -.
DR OMA; HCLFCGF; -.
DR BRENDA; 2.1.1.342; 2026.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR026332; HutW.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR13932; PTHR13932; 1.
DR PANTHER; PTHR13932:SF9; PTHR13932:SF9; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00311; heme_degradation_proteins_(Hut; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR04107; rSAM_HutW; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..445
FT /note="Anaerobilin synthase"
FT /id="PRO_0000446303"
FT DOMAIN 52..287
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 61
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
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 71
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 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 74
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 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 119..120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 190
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P32131"
SQ SEQUENCE 445 AA; 49549 MW; 28A8D846102F4ED6 CRC64;
MNANNTLDLT PHFALDGDQP FKDRRAMMPF RGAIPVAKEQ LAQTWQEMIN QTASPRKRLV
YLHIPFCATH CTFCGFYQNR FNEDACAHYT DALIREIEME ADSVLHQSAP IHAVYFGGGT
PSALSAHDLA RIITTLREKL PLAPDCEITI EGRVLNFDAE RIDACLDAGA NRFSIGIQSF
NSKIRKKMAR TSDGPTAIAF MESLVKRDRA AVVCDLLFGL PGQDAQTWGE DLAIARDIGL
DGVDLYALNV LSNTPLGKAV ENGRTTVPSP AERRDLYLQG CDFMDDAGWR CISNSHWGRT
TRERNLYNLL IKQGADCLAF GSGAGGSING YSWMNERNLQ TWHESVAAGK KPLMLIMRNA
ERNAQWRHTL QSGVETARVP LDELTPHAEK LAPLLAQWHQ KGLSRDASTC LRLTNEGRFW
ASNILQSLNE LIQVLNAPAI MREKP
