NDOB_PSEPU
ID NDOB_PSEPU Reviewed; 449 AA.
AC P0A110; O07830; O33461; P23094; Q52124;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Naphthalene 1,2-dioxygenase system, large oxygenase component {ECO:0000305};
DE EC=1.14.12.12 {ECO:0000269|PubMed:10692370, ECO:0000269|PubMed:6874638};
DE AltName: Full=ISP NAP {ECO:0000303|PubMed:6874638};
DE AltName: Full=Naphthalene 1,2-dioxygenase ISP alpha {ECO:0000303|PubMed:6874638};
DE AltName: Full=Naphthalene 1,2-dioxygenase subunit alpha {ECO:0000303|PubMed:6874638};
DE Short=ND subunit alpha {ECO:0000303|PubMed:3243438};
DE Short=NDO subunit alpha {ECO:0000303|PubMed:9634695};
GN Name=ndoB {ECO:0000303|PubMed:3243438};
GN Synonyms=nahA3, nahAC {ECO:0000303|PubMed:8486285}, ndoC2;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid pDTG1, Plasmid NAH7, and Plasmid NPL1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 8368 / NCIMB 9816 / PG;
RX PubMed=3243438; DOI=10.1016/0378-1119(88)90500-8;
RA Kurkela S., Lehvaeslaiho H., Palva E.T., Teeri T.H.;
RT "Cloning, nucleotide sequence and characterization of genes encoding
RT naphthalene dioxygenase of Pseudomonas putida strain NCIB9816.";
RL Gene 73:355-362(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BS202; PLASMID=NPL1;
RX PubMed=2661326;
RA Boronin A.M., Tsoi T.V., Kosheleva I.A., Arinbasarov M.U., Adanin V.M.;
RT "Cloning of Pseudomonas putida genes responsible for the primary stages of
RT oxidation of naphthalene in Escherichia coli cells.";
RL Genetika 25:226-237(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCIMB 9816-4; PLASMID=pDTG1;
RX PubMed=8973308; DOI=10.1016/s0378-1119(96)00462-3;
RA Parales J.V., Kumar A., Parales R.E., Gibson D.T.;
RT "Cloning and sequencing of the genes encoding 2-nitrotoluene dioxygenase
RT from Pseudomonas sp. JS42.";
RL Gene 181:57-61(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 17485 / DSM 50208 / JCM 6158 / NCIMB 12092 / Stanier 111 /
RC Biotype A; PLASMID=NAH7;
RX PubMed=8486285; DOI=10.1016/0378-1119(93)90613-8;
RA Simon M.J., Osslund T.D., Saunders R., Ensley B.D., Suggs S.,
RA Harcourt A.A., Suen W.-C., Cruden D.L., Gibson D.T., Zylstra G.J.;
RT "Sequences of genes encoding naphthalene dioxygenase in Pseudomonas putida
RT strains G7 and NCIB 9816-4.";
RL Gene 127:31-37(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 17484 / DSM 50222 / NCIMB 10535 / Stanier 110 / Biotype B;
RA Hamann C.;
RT "Naphthalene dioxygenase genes from Pseudomonas putida.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RC STRAIN=DSM 8368 / NCIMB 9816 / PG;
RX PubMed=6874638; DOI=10.1128/jb.155.2.505-511.1983;
RA Ensley B.D., Gibson D.T.;
RT "Naphthalene dioxygenase: purification and properties of a terminal
RT oxygenase component.";
RL J. Bacteriol. 155:505-511(1983).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASN-201; PHE-202; PHE-352;
RP TRP-358 AND ASP-362, PATHWAY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=NCIMB 9816-4;
RX PubMed=10692370; DOI=10.1128/jb.182.6.1641-1649.2000;
RA Parales R.E., Lee K., Resnick S.M., Jiang H., Lessner D.J., Gibson D.T.;
RT "Substrate specificity of naphthalene dioxygenase: effect of specific amino
RT acids at the active site of the enzyme.";
RL J. Bacteriol. 182:1641-1649(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH IRON ION AND
RP IRON-SULFUR (2FE-2S), COFACTOR, AND SUBUNIT.
RC STRAIN=NCIMB 9816-4;
RX PubMed=9634695; DOI=10.1016/s0969-2126(98)00059-8;
RA Kauppi B., Lee K., Carredano E., Parales R.E., Gibson D.T., Eklund H.,
RA Ramaswamy S.;
RT "Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-
RT dioxygenase.";
RL Structure 6:571-586(1998).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH IRON ION AND
RP IRON-SULFUR (2FE-2S), AND COFACTOR.
RC STRAIN=NCIMB 9816-4;
RX PubMed=10669618; DOI=10.1006/jmbi.1999.3462;
RA Carredano E., Karlsson A., Kauppi B., Choudhury D., Parales R.E.,
RA Parales J.V., Lee K., Gibson D.T., Eklund H., Ramaswamy S.;
RT "Substrate binding site of naphthalene 1,2-dioxygenase: functional
RT implications of indole binding.";
RL J. Mol. Biol. 296:701-712(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON ION;
RP IRON-SULFUR (2FE-2S); SUBSTRATE AND SUBSTRATE ANALOGS, COFACTOR, AND
RP SUBUNIT.
RX PubMed=12586937; DOI=10.1126/science.1078020;
RA Karlsson A., Parales J.V., Parales R.E., Gibson D.T., Eklund H.,
RA Ramaswamy S.;
RT "Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen
RT to iron.";
RL Science 299:1039-1042(2003).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH IRON ION;
RP IRON-SULFUR (2FE-2S) AND SUBSTRATE ANALOGS, COFACTOR, AND SUBUNIT.
RX PubMed=15942729; DOI=10.1007/s00775-005-0657-1;
RA Karlsson A., Parales J.V., Parales R.E., Gibson D.T., Eklund H.,
RA Ramaswamy S.;
RT "NO binding to naphthalene dioxygenase.";
RL J. Biol. Inorg. Chem. 10:483-489(2005).
CC -!- FUNCTION: Component of the naphthalene dioxygenase (NDO) multicomponent
CC enzyme system which catalyzes the incorporation of both atoms of
CC molecular oxygen into naphthalene to form cis-(1R,2S)-dihydroxy-1,2-
CC dihydronaphthalene. The alpha subunit has a catalytic role in the
CC holoenzyme. Also able to catalyze the cis-dihydroxylation of biphenyl
CC and phenanthrene (PubMed:10692370). {ECO:0000269|PubMed:10692370,
CC ECO:0000269|PubMed:6874638}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + naphthalene + O2 = (1R,2S)-1,2-
CC dihydronaphthalene-1,2-diol + NAD(+); Xref=Rhea:RHEA:19173,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16482,
CC ChEBI:CHEBI:44343, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.14.12.12; Evidence={ECO:0000269|PubMed:10692370,
CC ECO:0000269|PubMed:6874638};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10669618, ECO:0000269|PubMed:12586937,
CC ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:6874638,
CC ECO:0000269|PubMed:9634695};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:10669618,
CC ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729,
CC ECO:0000269|PubMed:6874638, ECO:0000269|PubMed:9634695};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:10669618, ECO:0000269|PubMed:12586937,
CC ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:9634695};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:10669618,
CC ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729,
CC ECO:0000269|PubMed:9634695};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC {ECO:0000305|PubMed:10692370}.
CC -!- SUBUNIT: The naphthalene dioxygenase (NDO) multicomponent enzyme system
CC is composed of an electron transfer component and a dioxygenase
CC component (iron sulfur protein (ISP)). The electron transfer component
CC is composed of a ferredoxin reductase (NdoR) and a ferredoxin (NdoA),
CC and the dioxygenase component is formed of a heterohexamer (trimer of
CC heterodimers) of three large alpha subunits (NdoB) and three small beta
CC subunits (NdoC). {ECO:0000269|PubMed:12586937,
CC ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:9634695,
CC ECO:0000305|PubMed:6874638}.
CC -!- INTERACTION:
CC P0A110; P0A112: ndoC; NbExp=7; IntAct=EBI-1029015, EBI-1029028;
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
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DR EMBL; M23914; AAB47591.1; -; Genomic_DNA.
DR EMBL; AF010471; AAB62707.1; -; Genomic_DNA.
DR EMBL; U49496; AAA92141.1; -; Genomic_DNA.
DR EMBL; M83949; AAA25902.1; -; Genomic_DNA.
DR EMBL; AF004284; AAB61373.1; -; Genomic_DNA.
DR PIR; JN0644; JN0644.
DR PIR; JS0071; JS0071.
DR RefSeq; NP_863072.1; NC_004999.1.
DR RefSeq; WP_011117400.1; NC_004999.1.
DR RefSeq; YP_534822.1; NC_007926.1.
DR PDB; 1EG9; X-ray; 1.60 A; A=1-449.
DR PDB; 1NDO; X-ray; 2.25 A; A/C/E=1-449.
DR PDB; 1O7G; X-ray; 1.70 A; A=1-449.
DR PDB; 1O7H; X-ray; 2.20 A; A=1-449.
DR PDB; 1O7M; X-ray; 1.75 A; A=1-449.
DR PDB; 1O7N; X-ray; 1.40 A; A=1-449.
DR PDB; 1O7P; X-ray; 1.95 A; A=1-449.
DR PDB; 1O7W; X-ray; 1.90 A; A=1-449.
DR PDB; 1UUV; X-ray; 1.65 A; A=1-449.
DR PDB; 1UUW; X-ray; 2.30 A; A=1-449.
DR PDBsum; 1EG9; -.
DR PDBsum; 1NDO; -.
DR PDBsum; 1O7G; -.
DR PDBsum; 1O7H; -.
DR PDBsum; 1O7M; -.
DR PDBsum; 1O7N; -.
DR PDBsum; 1O7P; -.
DR PDBsum; 1O7W; -.
DR PDBsum; 1UUV; -.
DR PDBsum; 1UUW; -.
DR AlphaFoldDB; P0A110; -.
DR SMR; P0A110; -.
DR IntAct; P0A110; 1.
DR DrugBank; DB08264; (1R, 2S)-cis 1,2 dihydroxy-1,2-dihydronaphthalene.
DR BioCyc; MetaCyc:MON-12802; -.
DR BRENDA; 1.14.12.12; 5092.
DR UniPathway; UPA00082; -.
DR EvolutionaryTrace; P0A110; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0018625; F:naphthalene 1,2-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08881; RHO_alpha_C_NDO-like; 1.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR043266; RHO_NdoB-like_C.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR015879; Ring_hydroxy_dOase_asu_C_dom.
DR InterPro; IPR001663; Rng_hydr_dOase-A.
DR PANTHER; PTHR43756; PTHR43756; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF00848; Ring_hydroxyl_A; 1.
DR PRINTS; PR00090; RNGDIOXGNASE.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Aromatic hydrocarbons catabolism; Dioxygenase; Iron;
KW Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Plasmid.
FT CHAIN 1..449
FT /note="Naphthalene 1,2-dioxygenase system, large oxygenase
FT component"
FT /id="PRO_0000085053"
FT DOMAIN 39..137
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 81
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10669618,
FT ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729,
FT ECO:0000269|PubMed:9634695, ECO:0007744|PDB:1EG9,
FT ECO:0007744|PDB:1NDO, ECO:0007744|PDB:1O7G,
FT ECO:0007744|PDB:1O7H, ECO:0007744|PDB:1O7M,
FT ECO:0007744|PDB:1O7N, ECO:0007744|PDB:1O7P,
FT ECO:0007744|PDB:1O7W, ECO:0007744|PDB:1UUV,
FT ECO:0007744|PDB:1UUW"
FT BINDING 83
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10669618,
FT ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729,
FT ECO:0000269|PubMed:9634695, ECO:0007744|PDB:1EG9,
FT ECO:0007744|PDB:1NDO, ECO:0007744|PDB:1O7G,
FT ECO:0007744|PDB:1O7H, ECO:0007744|PDB:1O7M,
FT ECO:0007744|PDB:1O7N, ECO:0007744|PDB:1O7P,
FT ECO:0007744|PDB:1O7W, ECO:0007744|PDB:1UUV,
FT ECO:0007744|PDB:1UUW"
FT BINDING 101
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10669618,
FT ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729,
FT ECO:0000269|PubMed:9634695, ECO:0007744|PDB:1EG9,
FT ECO:0007744|PDB:1NDO, ECO:0007744|PDB:1O7G,
FT ECO:0007744|PDB:1O7H, ECO:0007744|PDB:1O7M,
FT ECO:0007744|PDB:1O7N, ECO:0007744|PDB:1O7P,
FT ECO:0007744|PDB:1O7W, ECO:0007744|PDB:1UUV,
FT ECO:0007744|PDB:1UUW"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000269|PubMed:10669618,
FT ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729,
FT ECO:0000269|PubMed:9634695, ECO:0007744|PDB:1EG9,
FT ECO:0007744|PDB:1NDO, ECO:0007744|PDB:1O7G,
FT ECO:0007744|PDB:1O7H, ECO:0007744|PDB:1O7M,
FT ECO:0007744|PDB:1O7N, ECO:0007744|PDB:1O7P,
FT ECO:0007744|PDB:1O7W, ECO:0007744|PDB:1UUV,
FT ECO:0007744|PDB:1UUW"
FT BINDING 208
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:10669618,
FT ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729,
FT ECO:0000269|PubMed:9634695, ECO:0007744|PDB:1EG9,
FT ECO:0007744|PDB:1NDO, ECO:0007744|PDB:1O7G,
FT ECO:0007744|PDB:1O7H, ECO:0007744|PDB:1O7M,
FT ECO:0007744|PDB:1O7N, ECO:0007744|PDB:1O7P,
FT ECO:0007744|PDB:1O7W, ECO:0007744|PDB:1UUV,
FT ECO:0007744|PDB:1UUW"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:10669618,
FT ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729,
FT ECO:0000269|PubMed:9634695, ECO:0007744|PDB:1EG9,
FT ECO:0007744|PDB:1NDO, ECO:0007744|PDB:1O7G,
FT ECO:0007744|PDB:1O7H, ECO:0007744|PDB:1O7M,
FT ECO:0007744|PDB:1O7N, ECO:0007744|PDB:1O7P,
FT ECO:0007744|PDB:1O7W, ECO:0007744|PDB:1UUV,
FT ECO:0007744|PDB:1UUW"
FT BINDING 362
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:10669618,
FT ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729,
FT ECO:0000269|PubMed:9634695, ECO:0007744|PDB:1EG9,
FT ECO:0007744|PDB:1NDO, ECO:0007744|PDB:1O7G,
FT ECO:0007744|PDB:1O7H, ECO:0007744|PDB:1O7M,
FT ECO:0007744|PDB:1O7N, ECO:0007744|PDB:1O7P,
FT ECO:0007744|PDB:1O7W, ECO:0007744|PDB:1UUV"
FT SITE 352
FT /note="Important for enantioselectivity"
FT /evidence="ECO:0000269|PubMed:10692370"
FT VARIANT 4
FT /note="N -> K (in strain: G7)"
FT VARIANT 12
FT /note="S -> F (in strain: ATCC 17484)"
FT VARIANT 15
FT /note="S -> T (in strain: G7)"
FT VARIANT 32
FT /note="K -> R (in strain: G7)"
FT VARIANT 50
FT /note="A -> S (in strain: G7)"
FT VARIANT 70
FT /note="N -> S (in strain: G7)"
FT VARIANT 90..91
FT /note="SV -> NA (in strain: G7)"
FT VARIANT 122
FT /note="D -> E (in strain: G7)"
FT VARIANT 173
FT /note="M -> I (in strain: G7)"
FT VARIANT 225
FT /note="S -> A (in strain: G7)"
FT VARIANT 225
FT /note="S -> C (in strain: BS202)"
FT VARIANT 232
FT /note="A -> V (in strain: G7)"
FT VARIANT 275
FT /note="A -> S (in strain: G7)"
FT VARIANT 391
FT /note="E -> K (in strain: G7)"
FT VARIANT 421
FT /note="Q -> R (in strain: ATCC 17484)"
FT VARIANT 434
FT /note="H -> D (in strain: G7)"
FT MUTAGEN 201
FT /note="N->A: Unable to catalyze the cis-dihydroxylation of
FT biphenyl."
FT /evidence="ECO:0000269|PubMed:10692370"
FT MUTAGEN 202
FT /note="F->L: Unable to catalyze the cis-dihydroxylation of
FT naphthalene, biphenyl and phenanthrene."
FT /evidence="ECO:0000269|PubMed:10692370"
FT MUTAGEN 352
FT /note="F->L: Cis-dihydroxylation of naphthalene results in
FT the formation of cis-naphthalene dihydrodiol with altered
FT stereochemistry. Cis-dihydroxylation of biphenyl results in
FT the formation of cis-biphenyl 3,4-dihydrodiol as the major
FT product."
FT /evidence="ECO:0000269|PubMed:10692370"
FT MUTAGEN 352
FT /note="F->V: Cis-dihydroxylation of naphthalene results in
FT the formation of cis-naphthalene dihydrodiol with altered
FT stereochemistry. Cis-dihydroxylation of biphenyl and
FT phenanthrene results in the formation of cis-biphenyl 3,4-
FT dihydrodiol and cis-phenanthrene 1,2-dihydrodiol as the
FT major product, respectively."
FT /evidence="ECO:0000269|PubMed:10692370"
FT MUTAGEN 358
FT /note="W->A: Unable to catalyze the cis-dihydroxylation of
FT biphenyl. Preferentially oxidizes phenanthrene at the C-3
FT and C-4 positions, forming almost no cis-phenanthrene 1,2-
FT dihydrodiol."
FT /evidence="ECO:0000269|PubMed:10692370"
FT MUTAGEN 362
FT /note="D->A: Unable to catalyze the cis-dihydroxylation of
FT naphthalene, biphenyl and phenanthrene."
FT /evidence="ECO:0000269|PubMed:10692370"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 180..193
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 266..284
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 323..333
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 357..372
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 376..380
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:1O7N"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 411..424
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 429..435
FT /evidence="ECO:0007829|PDB:1O7N"
FT TURN 436..438
FT /evidence="ECO:0007829|PDB:1O7N"
FT HELIX 439..444
FT /evidence="ECO:0007829|PDB:1O7N"
SQ SEQUENCE 449 AA; 49608 MW; 1FD2F42296B4F7A8 CRC64;
MNYNNKILVS ESGLSQKHLI HGDEELFQHE LKTIFARNWL FLTHDSLIPA PGDYVTAKMG
IDEVIVSRQN DGSIRAFLNV CRHRGKTLVS VEAGNAKGFV CSYHGWGFGS NGELQSVPFE
KDLYGESLNK KCLGLKEVAR VESFHGFIYG CFDQEAPPLM DYLGDAAWYL EPMFKHSGGL
ELVGPPGKVV IKANWKAPAE NFVGDAYHVG WTHASSLRSG ESIFSSLAGN AALPPEGAGL
QMTSKYGSGM GVLWDGYSGV HSADLVPELM AFGGAKQERL NKEIGDVRAR IYRSHLNCTV
FPNNSMLTCS GVFKVWNPID ANTTEVWTYA IVEKDMPEDL KRRLADSVQR TFGPAGFWES
DDNDNMETAS QNGKKYQSRD SDLLSNLGFG EDVYGDAVYP GVVGKSAIGE TSYRGFYRAY
QAHVSSSNWA EFEHASSTWH TELTKTTDR
