ID A0A1Q8TF61_9GAMM Unreviewed; 438 AA.
AC A0A1Q8TF61;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=BTW10_05220 {ECO:0000313|EMBL:OLO12302.1};
OS Chromohalobacter japonicus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=223900 {ECO:0000313|EMBL:OLO12302.1, ECO:0000313|Proteomes:UP000186806};
RN [1] {ECO:0000313|EMBL:OLO12302.1, ECO:0000313|Proteomes:UP000186806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMB17 {ECO:0000313|EMBL:OLO12302.1,
RC ECO:0000313|Proteomes:UP000186806};
RA Mavrodi D.V., Olsson B.E., Korsakova E.S., Pyankova A., Mavrodi O.V.,
RA Plotnikova E.G.;
RT "Draft genome sequences of strains Salinicola socius SMB35, Salinicola sp.
RT MH3R3-1 and Chromohalobacter sp. SMB17 from the Verkhnekamsk potash mining
RT region of Russia.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homodimer. Part of a ferrous iron transporter composed of
CC EfeU, EfeO and EfeB. {ECO:0000256|RuleBase:RU365017}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU365017}.
CC -!- SIMILARITY: Belongs to the DyP-type peroxidase family. EfeB subfamily.
CC {ECO:0000256|ARBA:ARBA00005365}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLO12302.1}.
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DR EMBL; MSDQ01000007; OLO12302.1; -; Genomic_DNA.
DR RefSeq; WP_075368499.1; NZ_MSDQ01000007.1.
DR AlphaFoldDB; A0A1Q8TF61; -.
DR STRING; 223900.GCA_000821045_00606; -.
DR Proteomes; UP000186806; Unassembled WGS sequence.
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 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 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365017};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU365017}; Periplasm {ECO:0000256|RuleBase:RU365017};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU365017};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 71..221
FT /note="Dyp-type peroxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04261"
FT DOMAIN 237..418
FT /note="Dyp-type peroxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20628"
FT REGION 44..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 438 AA; 47840 MW; CCD74870FD02A39C CRC64;
MSDLSDNTPR CPFTLDRRRF LQGLGAAGAA AGLGGSAWAE SRTDAASSHD VTGAPVSTTT
QQSHPFHGRH QQGILTPRPA TGMVVVCDVL ARDRAGLERL LRILTERIAF LTQGGTYPKR
DPSYPPADSG ILGPTIAPDA LTVTVSLGAS VFDERFGLAD AKPKHLQRMT GFPNDALEPT
RCHGDLSLQI CANTHDTTIH ALRDIIKQTP GLLMVRWKQE GTVPVMPPSP DTPTPSARNY
LGFRDGTANP NTDDDALMDS LIWTGDDPDE PNWARGGSYQ VVRIIRNFVE RWDRAQLAEQ
EAIFGRRKES GAPLSGGSEY DKPNYNDDAD GKITPLDAHI RLANPRTPGF EKHRILRRPF
NYSNGVEANG QLDMGLLFIV YQADLEAGFI TVQSRLNGEP LEEYIKPVGG GYFFTLPGAI
DEHDFLGRTL LEATETDV
//
