METRE_DESRM
ID METRE_DESRM Reviewed; 668 AA.
AC A4J778;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Metal reductase {ECO:0000303|PubMed:25389064};
DE EC=1.16.1.- {ECO:0000269|PubMed:25389064};
GN OrderedLocusNames=Dred_2421 {ECO:0000312|EMBL:ABO50931.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP DOMAIN, AND COFACTOR.
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RX PubMed=26454174; DOI=10.1016/j.bbrc.2015.10.016;
RA Li Z., Kim D.D., Nelson O.D., Otwell A.E., Richardson R.E., Callister S.J.,
RA Lin H.;
RT "Molecular dissection of a putative iron reductase from Desulfotomaculum
RT reducens MI-1.";
RL Biochem. Biophys. Res. Commun. 467:503-508(2015).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RX PubMed=25389064; DOI=10.1111/1462-2920.12673;
RA Otwell A.E., Sherwood R.W., Zhang S., Nelson O.D., Li Z., Lin H.,
RA Callister S.J., Richardson R.E.;
RT "Identification of proteins capable of metal reduction from the proteome of
RT the Gram-positive bacterium Desulfotomaculum reducens MI-1 using an NADH-
RT based activity assay.";
RL Environ. Microbiol. 17:1977-1990(2015).
CC -!- FUNCTION: Metal reductase able to reduce Fe(III)-chelates to Fe(II)-
CC chelates, as well as soluble Cr(VI) and U(VI), using NADH as electron
CC donor. Cannot use NADPH as an electron donor. Is unable to reduce
CC riboflavin and FMN with NADH as electron donor. May have an in vivo
CC role in metal reduction in D.reducens, which is an organism capable of
CC reducing contaminant heavy metals and radionuclides.
CC {ECO:0000269|PubMed:25389064}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:25389064, ECO:0000269|PubMed:26454174};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:25389064, ECO:0000269|PubMed:26454174};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:26454174};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:25389064}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:25389064}.
CC -!- DOMAIN: Has an FMN-binding N-terminal domain (NTD), an FAD-binding C-
CC terminal domain (CTD), and a 4Fe-4S cluster between the two domains.
CC CTD is the main contributor to the iron-reduction activity, and NTD and
CC the 4Fe-4S cluster are not directly involved in such activity.
CC {ECO:0000269|PubMed:26454174}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC oxidoreductase/NADH oxidase family. {ECO:0000305}.
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DR EMBL; CP000612; ABO50931.1; -; Genomic_DNA.
DR RefSeq; WP_011878729.1; NC_009253.1.
DR AlphaFoldDB; A4J778; -.
DR SMR; A4J778; -.
DR STRING; 349161.Dred_2421; -.
DR EnsemblBacteria; ABO50931; ABO50931; Dred_2421.
DR KEGG; drm:Dred_2421; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_2_9; -.
DR OMA; GWVHRAH; -.
DR OrthoDB; 1308229at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cytoplasm; FAD; Flavoprotein; FMN; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..668
FT /note="Metal reductase"
FT /id="PRO_0000439795"
FT BINDING 23..25
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 57
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 98
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 216
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 290
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 312..313
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 336
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 339
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 343
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 355
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 386
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 405
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 413
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 423
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
FT BINDING 450
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P42593"
SQ SEQUENCE 668 AA; 71851 MW; 7980966DD3569573 CRC64;
MSILFSPAQI GTLQLRNRII MTPMHLGYTP NGEVTDQLIE FYRVRARGGA GLIVVGGCGI
DRIGNAYGMT QLDDDRFIPG LRRLADAVQA EGAKIVAQLY QAGRYAHSAL TGQPAVAPSP
IPSKLTGETP VELTEEKIAE IVASFAKAAK RAKTAGFDGV EIIASAGYLI SQFLSPLTNK
RTDRYGGDLQ ARMTFGLEVV AAVREAVGSD YPIIVRVAGN DFMPGSHTNT EAQVFCQAME
KSGVNAINVT GGWHETQVPQ ITMNVPPGAY AYLAYGIKQA VSIPVIACNR INTPDLAEAI
LQEGKADFIG MARSLMADPE LPNKAMSGHP EQIRPCIGCN QGCLDHVFRM KPVSCLVNAE
AGREAELSLT PTSQPGKILV IGAGAAGLEF ARVAALRGHK VTIWEESDQA GGQLILAAAP
PGRKDFLHLR TYLVNACRDL GVEIQYHTKA TPENILSAVQ EGKFNRVVIA TGAHPITPPI
PIEEGVKVIQ AWDVLAGRSK AGQNIIIVGG GAVGVETALL LAESGTLDNE TLRFLMLQQA
ETEKELYRLL IQGTKKITVL EMANGIGRDI GPSTRWSMLA DLKRHQVNCL DETTVLEIRR
EGVLVKNAGT QKILPADTVI LAVGSRSQNE LYQALQGKVE YLSIIGDAIK PRKVMDAIHQ
AYNEAIKY
