FPRA_MOOTA
ID FPRA_MOOTA Reviewed; 399 AA.
AC Q9FDN7; Q2RIY8;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Nitric oxide reductase;
DE EC=1.-.-.-;
DE AltName: Full=FMN protein FprA;
DE AltName: Full=Flavoprotein A;
DE AltName: Full=Type A flavoprotein FprA;
GN Name=fprA; OrderedLocusNames=Moth_1287;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11160086; DOI=10.1128/jb.183.5.1560-1567.2001;
RA Das A., Coulter E.D., Kurtz D.M. Jr., Ljungdahl L.G.;
RT "Five-gene cluster in Clostridium thermoaceticum consisting of two
RT divergent operons encoding rubredoxin oxidoreductase-rubredoxin and
RT rubrerythrin-type A flavoprotein- high-molecular-weight rubredoxin.";
RL J. Bacteriol. 183:1560-1567(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
RN [3]
RP IDENTIFICATION OF FUNCTION, CHARACTERIZATION, AND COFACTOR.
RX PubMed=12627946; DOI=10.1021/bi027253k;
RA Silaghi-Dumitrescu R., Coulter E.D., Das A., Ljungdahl L.G.,
RA Jameson G.N.L., Huynh B.H., Kurtz D.M. Jr.;
RT "A flavodiiron protein and high molecular weight rubredoxin from Moorella
RT thermoacetica with nitric oxide reductase activity.";
RL Biochemistry 42:2806-2815(2003).
CC -!- FUNCTION: Has nitric oxide reductase activity in combination with Hrb;
CC probably involved in nitrosative stress protection.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:12627946};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:12627946};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:12627946};
CC Note=Binds 2 iron ions per subunit. {ECO:0000269|PubMed:12627946};
CC -!- SUBUNIT: Homodimer.
CC -!- INDUCTION: Constitutively expressed.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000305}.
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DR EMBL; AF202316; AAG00802.1; -; Genomic_DNA.
DR EMBL; CP000232; ABC19601.1; -; Genomic_DNA.
DR RefSeq; WP_011392801.1; NC_007644.1.
DR RefSeq; YP_430144.1; NC_007644.1.
DR PDB; 1YCF; X-ray; 3.00 A; A/B/C/D=2-399.
DR PDB; 1YCG; X-ray; 2.80 A; A/B/C/D=2-399.
DR PDB; 1YCH; X-ray; 2.80 A; A/B/C/D=2-399.
DR PDBsum; 1YCF; -.
DR PDBsum; 1YCG; -.
DR PDBsum; 1YCH; -.
DR AlphaFoldDB; Q9FDN7; -.
DR SMR; Q9FDN7; -.
DR STRING; 264732.Moth_1287; -.
DR DrugBank; DB03247; Flavin mononucleotide.
DR EnsemblBacteria; ABC19601; ABC19601; Moth_1287.
DR KEGG; mta:Moth_1287; -.
DR PATRIC; fig|264732.11.peg.1381; -.
DR eggNOG; COG0426; Bacteria.
DR HOGENOM; CLU_017490_0_0_9; -.
DR EvolutionaryTrace; Q9FDN7; -.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR016440; Rubredoxin-O_OxRdtase.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005243; ROO; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Flavoprotein; FMN; Iron; Metal-binding;
KW Oxidoreductase; Transport.
FT CHAIN 1..399
FT /note="Nitric oxide reductase"
FT /id="PRO_0000216805"
FT DOMAIN 255..394
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 32..221
FT /note="Zinc metallo-hydrolase"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:1YCG"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1YCG"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1YCG"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 185..199
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 204..216
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 236..248
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 253..259
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 265..279
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 338..348
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1YCG"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:1YCG"
FT HELIX 380..397
FT /evidence="ECO:0007829|PDB:1YCG"
SQ SEQUENCE 399 AA; 44297 MW; 198C380C41C58614 CRC64;
MSQPVAITDG IYWVGAVDWN IRYFHGPAFS THRGTTYNAY LIVDDKTALV DTVYEPFKEE
LIAKLKQIKD PVKLDYLVVN HTESDHAGAF PAIMELCPDA HVLCTQRAFD SLKAHYSHID
FNYTIVKTGT SVSLGKRSLT FIEAPMLHWP DSMFTYVPEE ALLLPNDAFG QHIATSVRFD
DQVDAGLIMD EAAKYYANIL MPFSNLITKK LDEIQKINLA IKTIAPSHGI IWRKDPGRII
EAYARWAEGQ GKAKAVIAYD TMWLSTEKMA HALMDGLVAG GCEVKLFKLS VSDRNDVIKE
ILDARAVLVG SPTINNDILP VVSPLLDDLV GLRPKNKVGL AFGAYGWGGG AQKILEERLK
AAKIELIAEP GPTVQWVPRG EDLQRCYELG RKIAARIAD
