ID C7NBZ8_LEPBD Unreviewed; 412 AA.
AC C7NBZ8;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Deferrochelatase {ECO:0000256|ARBA:ARBA00033771, ECO:0000256|RuleBase:RU365017};
DE EC=1.11.1.- {ECO:0000256|RuleBase:RU365017};
DE AltName: Full=Peroxidase EfeB {ECO:0000256|ARBA:ARBA00033775, ECO:0000256|RuleBase:RU365017};
GN OrderedLocusNames=Lebu_1813 {ECO:0000313|EMBL:ACV39679.1};
OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS 10249 / C-1013-b).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV39679.1, ECO:0000313|Proteomes:UP000001910};
RN [1] {ECO:0000313|EMBL:ACV39679.1, ECO:0000313|Proteomes:UP000001910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b
RC {ECO:0000313|Proteomes:UP000001910};
RX PubMed=21304648; DOI=10.4056/sigs.1854;
RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT b).";
RL Stand. Genomic Sci. 1:126-132(2009).
CC -!- FUNCTION: Involved in the recovery of exogenous heme iron. Extracts
CC iron from heme while preserving the protoporphyrin ring intact.
CC {ECO:0000256|RuleBase:RU365017}.
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:0000256|ARBA:ARBA00034258};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22585;
CC Evidence={ECO:0000256|ARBA:ARBA00034258};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|RuleBase:RU365017};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently
CC per subunit. {ECO:0000256|RuleBase:RU365017};
CC -!- SIMILARITY: Belongs to the DyP-type peroxidase family.
CC {ECO:0000256|RuleBase:RU365017}.
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DR EMBL; CP001685; ACV39679.1; -; Genomic_DNA.
DR RefSeq; WP_015770018.1; NC_013192.1.
DR AlphaFoldDB; C7NBZ8; -.
DR STRING; 523794.Lebu_1813; -.
DR KEGG; lba:Lebu_1813; -.
DR eggNOG; COG2837; Bacteria.
DR HOGENOM; CLU_039488_2_0_0; -.
DR OrthoDB; 9781066at2; -.
DR Proteomes; UP000001910; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01413; Dyp_perox_fam; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 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 Pfam; PF10518; TAT_signal; 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 {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU365017};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365017};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365017};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365017};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU365017};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..216
FT /note="Dyp-type peroxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04261"
FT DOMAIN 225..399
FT /note="Dyp-type peroxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20628"
SQ SEQUENCE 412 AA; 46408 MW; 7579A69DF0045E06 CRC64;
MSDENDKKWF DKKISRRDFL KKAGMVGAGA AIGASGASAI FANMFSGKAN QVVGNEKISF
YGEHQSGIAT PVQKNVYFAV LDLHSMDKEE IKQMFKDWTD YSEKLMKGEL VAPELANHLV
PPLDTGETVG LNPYRLTITF GISPSFLDKL KMDNKKMEEF KDLPHFPRDQ IKDKYKGGDI
CIQACADDAQ VAFHAVRNLV RKGRALITLK WTQAGFLPIG NGKETPRNLF GFKDGTENPK
NDNDFKNVVW YDKDNWLKNG TFLIVRRIQM HLETWDRTNL QEQENTFGRY KESGAPFGET
DEFATIDINK KGPDGKPVLP IDSHVYLAKK ADVKIARRAF SYSNGIDEVS GQFDAGLLFI
CFQKHPDQFI KIQNSLGNDD KLNEYITHVG TGIFACFGGI KKGEYIGQKL FE
//
