EFEB_ECO57
ID EFEB_ECO57 Reviewed; 423 AA.
AC Q8XAS4; Q7AFM4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Deferrochelatase {ECO:0000305|PubMed:21324904};
DE EC=4.99.1.1 {ECO:0000269|PubMed:21324904};
DE AltName: Full=Peroxidase EfeB {ECO:0000305|PubMed:21324904};
DE EC=1.11.1.- {ECO:0000269|PubMed:21324904};
DE Flags: Precursor;
GN Name=efeB; Synonyms=ycdB; OrderedLocusNames=Z1521, ECs1265;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP SUBUNIT.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=17627767; DOI=10.1111/j.1365-2958.2007.05802.x;
RA Cao J., Woodhall M.R., Alvarez J., Cartron M.L., Andrews S.C.;
RT "EfeUOB (YcdNOB) is a tripartite, acid-induced and CpxAR-regulated, low-pH
RT Fe2+ transporter that is cryptic in Escherichia coli K-12 but functional in
RT E. coli O157:H7.";
RL Mol. Microbiol. 65:857-875(2007).
RN [4] {ECO:0007744|PDB:3O72}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 36-423 IN COMPLEX WITH HEME,
RP FUNCTION AS A DEFERROCHELATASE AND PEROXIDASE, CATALYTIC ACTIVITY,
RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF GLN-68; GLY-223; PRO-227; ASP-235;
RP GLY-236; ASN-239; HIS-329; LEU-346; ARG-347; GLY-349; SER-351; LEU-366 AND
RP PHE-368.
RC STRAIN=O157:H7 / EHEC;
RX PubMed=21324904; DOI=10.1074/jbc.m110.197780;
RA Liu X., Du Q., Wang Z., Zhu D., Huang Y., Li N., Wei T., Xu S., Gu L.;
RT "Crystal structure and biochemical features of EfeB/YcdB from Escherichia
RT coli O157: ASP235 plays divergent roles in different enzyme-catalyzed
RT processes.";
RL J. Biol. Chem. 286:14922-14931(2011).
CC -!- FUNCTION: Involved in the recovery of exogenous heme iron. Extracts
CC iron from heme while preserving the protoporphyrin ring intact. Also
CC displays peroxidase activity on guaiacol and catechol in vitro. The
CC deferrochelatase activity appears to be closely related to the
CC peroxidation activity, but the link is unclear.
CC {ECO:0000269|PubMed:21324904}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + heme b = Fe(2+) + protoporphyrin IX;
CC Xref=Rhea:RHEA:22584, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:60344; EC=4.99.1.1;
CC Evidence={ECO:0000269|PubMed:21324904};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22585;
CC Evidence={ECO:0000269|PubMed:21324904};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:21324904};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC per subunit. {ECO:0000269|PubMed:21324904};
CC -!- SUBUNIT: The heme-bound EfeB forms a homodimer whereas the apo-form
CC mainly exists as a monomer. Part of a ferrous iron transporter composed
CC of EfeU, EfeO and EfeB. {ECO:0000269|PubMed:17627767,
CC ECO:0000269|PubMed:21324904}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the DyP-type peroxidase family. EfeB subfamily.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG55637.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34688.1; -; Genomic_DNA.
DR PIR; A85647; A85647.
DR PIR; A99787; A99787.
DR RefSeq; NP_309292.1; NC_002695.1.
DR RefSeq; WP_001199176.1; NZ_SEKU01000016.1.
DR PDB; 3O72; X-ray; 1.95 A; A/B/C/D=36-423.
DR PDBsum; 3O72; -.
DR AlphaFoldDB; Q8XAS4; -.
DR SMR; Q8XAS4; -.
DR STRING; 155864.EDL933_1445; -.
DR PeroxiBase; 5880; EcoH7DyPrx01.
DR EnsemblBacteria; AAG55637; AAG55637; Z1521.
DR EnsemblBacteria; BAB34688; BAB34688; ECs_1265.
DR GeneID; 912778; -.
DR KEGG; ece:Z1521; -.
DR KEGG; ecs:ECs_1265; -.
DR PATRIC; fig|386585.9.peg.1372; -.
DR eggNOG; COG2837; Bacteria.
DR HOGENOM; CLU_039488_0_0_6; -.
DR OMA; QACANDP; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004325; F:ferrochelatase activity; IEA:RHEA.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0033212; P:iron import into cell; IEA:InterPro.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR006314; Dyp_peroxidase.
DR InterPro; IPR006313; EfeB.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF04261; Dyp_perox; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR TIGRFAMs; TIGR01413; Dyp_perox_fam; 1.
DR TIGRFAMs; TIGR01412; tat_substr_1; 1.
DR PROSITE; PS51404; DYP_PEROXIDASE; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Heme; Iron; Lyase; Metal-binding; Oxidoreductase; Periplasm;
KW Peroxidase; Reference proteome; Signal.
FT SIGNAL 1..35
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 36..423
FT /note="Deferrochelatase"
FT /id="PRO_0000278544"
FT BINDING 236..238
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:21324904,
FT ECO:0007744|PDB:3O72"
FT BINDING 329
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="proximal binding residue"
FT /evidence="ECO:0000269|PubMed:21324904,
FT ECO:0007744|PDB:3O72"
FT BINDING 334..336
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:21324904,
FT ECO:0007744|PDB:3O72"
FT BINDING 347
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000269|PubMed:21324904,
FT ECO:0007744|PDB:3O72"
FT MUTAGEN 68
FT /note="Q->W: Loss of deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 223
FT /note="G->F: Loss of deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 227
FT /note="P->F: Loss of deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 235
FT /note="D->A: Large decrease in deferrochelatase activity
FT and peroxidase activity on guaiacol and catechol. Still
FT binds heme."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 235
FT /note="D->N: No effect on deferrochelatase activity. No
FT effect on peroxidase activity on guaiacol, but loss of
FT peroxidase activity on catechol. Still binds heme."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 235
FT /note="D->W: Loss of deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 236
FT /note="G->F: Loss of deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 239
FT /note="N->W: Loss of deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 329
FT /note="H->A: Loss of deferrochelatase activity. Great
FT decrease in peroxidase activity on guaiacol, and loss of
FT peroxidase activity on catechol. Still binds heme."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 346
FT /note="L->W: Loss of deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 347
FT /note="R->E: Loss of deferrochelatase activity. Great
FT decrease in peroxidase activity on guaiacol, and loss of
FT peroxidase activity on catechol. Still binds heme."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 349
FT /note="G->F: Loss of deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 349
FT /note="G->L: Loss of deferrochelatase activity. Great
FT decrease in peroxidase activity on guaiacol and catechol.
FT Still binds heme."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 351
FT /note="S->Q: Large decrease in deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 366
FT /note="L->W: Loss of deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT MUTAGEN 368
FT /note="F->W: Loss of deferrochelatase activity."
FT /evidence="ECO:0000269|PubMed:21324904"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 70..79
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 84..103
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:3O72"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 186..198
FT /evidence="ECO:0007829|PDB:3O72"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:3O72"
FT TURN 221..223
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 268..277
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:3O72"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 362..373
FT /evidence="ECO:0007829|PDB:3O72"
FT TURN 375..378
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 379..386
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:3O72"
FT STRAND 395..405
FT /evidence="ECO:0007829|PDB:3O72"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:3O72"
SQ SEQUENCE 423 AA; 46620 MW; 256FB987670B750C CRC64;
MQYEDKNGVN EPSRRRLLKG IGALALAGSC PVAHAQKTQS APGTLSPVAR NEKQPFYGEH
QAGILTPQQA AMMLVAFDVL ASDKADLERL FRLLTQRFAF LTQGGAAPET PNPRLPPLDS
GILGGYIAPD NLTITLSVGH SLFDERFGLA PQMPKKLQKM TRFPNDSLDA ALCHGDVLLQ
ICANTQDTVI HALRDIIKHT PDLLSVRWKR EGFISDHAAR SKGKETPINL LGFKDGTANP
DSQNDKLMQK VVWVTADQQE PAWTIGGSYQ AVRLIQFRVE FWDRTPLKEQ QTIFGRDKQT
GAPLGMQHEH DVPDYASDPE GKGIALDSHI RLANPRTAES ESSLMLRRGY SYSLGVTNSG
QLDMGLLFVC YQHDLEKGFL TVQKRLNGEA LEEYVKPIGG GYFFALPGVK DANDYLGSAL
LRV
