ID EFEB_YERPS Reviewed; 434 AA.
AC Q66BP4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Deferrochelatase;
DE EC=4.98.1.1 {ECO:0000250|UniProtKB:P31545};
DE AltName: Full=Peroxidase EfeB;
DE EC=1.11.1.- {ECO:0000250|UniProtKB:P31545};
DE Flags: Precursor;
GN Name=efeB; OrderedLocusNames=YPTB1727;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
CC -!- FUNCTION: Involved in the recovery of exogenous heme iron. Extracts
CC iron from heme while preserving the protoporphyrin ring intact.
CC {ECO:0000250|UniProtKB:P31545}.
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=4.98.1.1;
CC Evidence={ECO:0000250|UniProtKB:P31545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22585;
CC Evidence={ECO:0000250|UniProtKB:P31545};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. Part of a ferrous iron transporter composed of
CC EfeU, EfeO and EfeB (By similarity). {ECO:0000250}.
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}.
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; BX936398; CAH20966.1; -; Genomic_DNA.
DR RefSeq; WP_011192194.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66BP4; -.
DR SMR; Q66BP4; -.
DR PeroxiBase; 5877; YpsDyPrx01_IP32953.
DR GeneID; 66841838; -.
DR KEGG; ypo:BZ17_773; -.
DR KEGG; yps:YPTB1727; -.
DR PATRIC; fig|273123.14.peg.818; -.
DR Proteomes; UP000001011; 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; IPR048328; Dyp_perox_C.
DR InterPro; IPR048327; Dyp_perox_N.
DR InterPro; IPR006314; Dyp_peroxidase.
DR InterPro; IPR006313; EfeB/EfeN.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR01413; Dyp_perox_fam; 1.
DR NCBIfam; TIGR01412; tat_substr_1; 1.
DR PANTHER; PTHR30521:SF4; DEFERROCHELATASE; 1.
DR PANTHER; PTHR30521; DEFERROCHELATASE/PEROXIDASE; 1.
DR Pfam; PF20628; Dyp_perox_C; 1.
DR Pfam; PF04261; Dyp_perox_N; 1.
DR SUPFAM; SSF54909; Dimeric alpha+beta barrel; 1.
DR PROSITE; PS51404; DYP_PEROXIDASE; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Heme; Iron; Lyase; Metal-binding; Oxidoreductase; Periplasm; Peroxidase;
KW Signal.
FT SIGNAL 1..45
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 46..434
FT /note="Deferrochelatase"
FT /id="PRO_0000278553"
FT BINDING 247..249
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P31545"
FT BINDING 340
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:0000250|UniProtKB:P31545"
FT BINDING 345..347
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P31545"
FT BINDING 358
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P31545"
SQ SEQUENCE 434 AA; 47815 MW; 5F0C4314573C0442 CRC64;
MRDKTGPKFG PYQPDDEAVS PSRRRLILGM GMVSGALVLG GAKTAQAADC RSPDVAGTQD
ERWQKQPFYG QHQAGVLTPQ QAAMMLVAFD VLATDKTSLI RLFKLLTERL AFLTTGGRAP
SVNAKLPPLD SGIMGPEIYP DNLTVTVSVG NALFDERFGL QGQKPLRLQR MTRFPNDSLD
AGLCHGDVML QICANTNETV IHALRDIIKH TPDLLSVRWK REGFISAHAA RSKGQETPIN
LLGFKDGTAN PKISNKPLIN NVVWVSNNAG EPAWAVGGSY QVVRIIRFKV EFWDRTPLQE
QQTIFGRDKN SGAPLGMQHE HDEPNYAKDP EGKVIPMDAH IRLANPRTIE TQRNLMLRRG
YSYSLGVSNS GQLDMGLLFV CYQSDLAQAF LTVQERLNGE ALEEYVKPIG GGYFFTLPGV
ADANHYLAQS LLEA
//
