NAPE_ENTFA
ID NAPE_ENTFA Reviewed; 447 AA.
AC P37062;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=NADH peroxidase;
DE Short=NPXase;
DE Short=Npx;
DE EC=1.11.1.1;
GN Name=npr; OrderedLocusNames=EF_1211;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1;
RX PubMed=1719212; DOI=10.1016/0022-2836(91)80180-3;
RA Ross R.P., Claiborne A.;
RT "Cloning, sequence and overexpression of NADH peroxidase from Streptococcus
RT faecalis 10C1. Structural relationship with the flavoprotein disulfide
RT reductases.";
RL J. Mol. Biol. 221:857-871(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [3]
RP PROTEIN SEQUENCE OF 1-51.
RC STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1;
RX PubMed=2501302; DOI=10.1016/s0021-9258(18)63861-x;
RA Poole L.B., Claiborne A.;
RT "The non-flavin redox center of the streptococcal NADH peroxidase. I. Thiol
RT reactivity and redox behavior in the presence of urea.";
RL J. Biol. Chem. 264:12322-12329(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS).
RC STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1;
RX PubMed=1942054; DOI=10.1016/0022-2836(91)90936-z;
RA Stehle T., Ahmed S.A., Claiborne A., Schulz G.E.;
RT "Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at
RT 2.16-A resolution.";
RL J. Mol. Biol. 221:1325-1344(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD AND FAD.
RC STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1;
RX PubMed=8425532; DOI=10.1111/j.1432-1033.1993.tb19889.x;
RA Stehle T., Claiborne A., Schulz G.E.;
RT "NADH binding site and catalysis of NADH peroxidase.";
RL Eur. J. Biochem. 211:221-226(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH FAD, ACTIVE SITE, AND
RP OXIDATION AT CYS-42.
RC STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1;
RX PubMed=8756456; DOI=10.1021/bi961037s;
RA Yeh J.I., Claiborne A., Hol W.G.J.;
RT "Structure of the native cysteine-sulfenic acid redox center of
RT enterococcal NADH peroxidase refined at 2.8-A resolution.";
RL Biochemistry 35:9951-9957(1996).
RN [7]
RP STRUCTURE BY NMR.
RC STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1;
RX PubMed=9214307; DOI=10.1021/bi9707990;
RA Crane E.J. III, Vervoort J., Clairborne A.;
RT "13C NMR analysis of the cysteine-sulfenic acid redox center of
RT enterococcal NADH peroxidase.";
RL Biochemistry 36:8611-8618(1997).
CC -!- FUNCTION: Peroxidase whose active site is a redox-active cysteine-
CC sulfenic acid.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O2 + NADH = 2 H2O + NAD(+); Xref=Rhea:RHEA:18509,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.11.1.1;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8425532,
CC ECO:0000269|PubMed:8756456}.
CC -!- MISCELLANEOUS: The active site is the redox-active Cys-42 oxidized to
CC Cys-SOH. The oxidized form is stabilized by a hydrogen bond formation
CC with His-10.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; X62755; CAA44611.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO81008.1; -; Genomic_DNA.
DR PIR; S18332; S18332.
DR RefSeq; NP_814938.1; NC_004668.1.
DR RefSeq; WP_002379347.1; NZ_KE136528.1.
DR PDB; 1F8W; X-ray; 2.45 A; A=1-447.
DR PDB; 1JOA; X-ray; 2.80 A; A=1-447.
DR PDB; 1NHP; X-ray; 2.00 A; A=1-447.
DR PDB; 1NHQ; X-ray; 2.00 A; A=1-447.
DR PDB; 1NHR; X-ray; 2.10 A; A=1-447.
DR PDB; 1NHS; X-ray; 2.00 A; A=1-447.
DR PDB; 1NPX; X-ray; 2.16 A; A=1-447.
DR PDB; 2NPX; X-ray; 2.40 A; A=1-447.
DR PDBsum; 1F8W; -.
DR PDBsum; 1JOA; -.
DR PDBsum; 1NHP; -.
DR PDBsum; 1NHQ; -.
DR PDBsum; 1NHR; -.
DR PDBsum; 1NHS; -.
DR PDBsum; 1NPX; -.
DR PDBsum; 2NPX; -.
DR AlphaFoldDB; P37062; -.
DR SMR; P37062; -.
DR STRING; 226185.EF_1211; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB03382; S-oxy-L-cysteine.
DR PeroxiBase; 4010; EfNadPrx01.
DR EnsemblBacteria; AAO81008; AAO81008; EF_1211.
DR KEGG; efa:EF1211; -.
DR PATRIC; fig|226185.45.peg.2288; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_0_9; -.
DR OMA; WVSHAPC; -.
DR BRENDA; 1.11.1.1; 2095.
DR SABIO-RK; P37062; -.
DR EvolutionaryTrace; P37062; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016692; F:NADH peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidation;
KW Oxidoreductase; Peroxidase; Redox-active center; Reference proteome.
FT CHAIN 1..447
FT /note="NADH peroxidase"
FT /id="PRO_0000184705"
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:8756456"
FT ACT_SITE 42
FT /note="Redox-active"
FT /evidence="ECO:0000269|PubMed:8756456"
FT BINDING 7..11
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8425532,
FT ECO:0000269|PubMed:8756456"
FT BINDING 32
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8425532,
FT ECO:0000269|PubMed:8756456"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8425532,
FT ECO:0000269|PubMed:8756456"
FT BINDING 110..113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8425532,
FT ECO:0000269|PubMed:8756456"
FT BINDING 132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8425532,
FT ECO:0000269|PubMed:8756456"
FT BINDING 160
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8425532"
FT BINDING 179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8425532"
FT BINDING 188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8425532"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8425532"
FT BINDING 281
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8425532,
FT ECO:0000269|PubMed:8756456"
FT BINDING 297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8425532"
FT BINDING 299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:8425532,
FT ECO:0000269|PubMed:8756456"
FT BINDING 328
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:8425532"
FT MOD_RES 42
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000269|PubMed:8756456"
FT CONFLICT 226
FT /note="I -> V (in Ref. 1; CAA44611)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 26..39
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1NHP"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1NHP"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1NHP"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:1NHP"
FT TURN 184..188
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:1NHP"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:1NHP"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1NHP"
FT TURN 288..291
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 354..363
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 372..379
FT /evidence="ECO:0007829|PDB:1NHP"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:1NHP"
FT STRAND 385..395
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 414..418
FT /evidence="ECO:0007829|PDB:1NHP"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:1NHP"
FT HELIX 434..445
FT /evidence="ECO:0007829|PDB:1NHP"
SQ SEQUENCE 447 AA; 49566 MW; 3FAF85AF5BB2A70B CRC64;
MKVIVLGSSH GGYEAVEELL NLHPDAEIQW YEKGDFISFL SCGMQLYLEG KVKDVNSVRY
MTGEKMESRG VNVFSNTEIT AIQPKEHQVT VKDLVSGEER VENYDKLIIS PGAVPFELDI
PGKDLDNIYL MRGRQWAIKL KQKTVDPEVN NVVVIGSGYI GIEAAEAFAK AGKKVTVIDI
LDRPLGVYLD KEFTDVLTEE MEANNITIAT GETVERYEGD GRVQKIVTDK NAYDADLVVV
AVGVRPNTAW LKGTLELHPN GLIKTDEYMR TSEPDVFAVG DATLIKYNPA DTEVNIALAT
NARKQGRFAV KNLEEPVKPF PGVQGSSGLA VFDYKFASTG INEVMAQKLG KETKAVTVVE
DYLMDFNPDK QKAWFKLVYD PETTQILGAQ LMSKADLTAN INAISLAIQA KMTIEDLAYA
DFFFQPAFDK PWNIINTAAL EAVKQER
