NARH_ECOLI
ID NARH_ECOLI Reviewed; 512 AA.
AC P11349;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Respiratory nitrate reductase 1 beta chain;
DE EC=1.7.5.1;
DE AltName: Full=Nitrate reductase A subunit beta;
DE AltName: Full=Quinol-nitrate oxidoreductase subunit beta;
GN Name=narH; OrderedLocusNames=b1225, JW1216;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / TG1;
RX PubMed=2674654; DOI=10.1007/bf00331275;
RA Blasco F., Iobbi C., Giordano G., Chippaux M., Bonnefoy V.;
RT "Nitrate reductase of Escherichia coli: completion of the nucleotide
RT sequence of the nar operon and reassessment of the role of the alpha and
RT beta subunits in iron binding and electron transfer.";
RL Mol. Gen. Genet. 218:249-256(1989).
RN [2]
RP SEQUENCE REVISION TO 398-417.
RC STRAIN=K12 / TG1;
RA Blasco F.;
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 365-512.
RX PubMed=2832376; DOI=10.1128/jb.170.4.1721-1729.1988;
RA Sodergren E.J., Demoss J.A.;
RT "narI region of the Escherichia coli nitrate reductase (nar) operon
RT contains two genes.";
RL J. Bacteriol. 170:1721-1729(1988).
RN [7]
RP PROTEIN SEQUENCE OF 1-10.
RX PubMed=3053688; DOI=10.1016/s0021-9258(18)37572-0;
RA Sodergren E.J., Hsu P.Y., Demoss J.A.;
RT "Roles of the narJ and narI gene products in the expression of nitrate
RT reductase in Escherichia coli.";
RL J. Biol. Chem. 263:16156-16162(1988).
RN [8]
RP EPR SPECTROSCOPY OF IRON-SULFUR CLUSTERS.
RX PubMed=1321049; DOI=10.1111/j.1432-1033.1992.tb17020.x;
RA Guigliarelli B., Asso M., More C., Augier V., Blasco F., Pommier J.,
RA Giordano G., Bertrand P.;
RT "EPR and redox characterization of iron-sulfur centers in nitrate
RT reductases A and Z from Escherichia coli. Evidence for a high-potential and
RT a low-potential class and their relevance in the electron-transfer
RT mechanism.";
RL Eur. J. Biochem. 207:61-68(1992).
RN [9]
RP MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR
RP CLUSTERS.
RX PubMed=8383531; DOI=10.1021/bi00059a018;
RA Augier V., Guigliarelli B., Asso M., Bertrand P., Frixon C., Giordano G.,
RA Chippaux M., Blasco F.;
RT "Site-directed mutagenesis of conserved cysteine residues within the beta
RT subunit of Escherichia coli nitrate reductase. Physiological, biochemical,
RT and EPR characterization of the mutated enzymes.";
RL Biochemistry 32:2013-2023(1993).
RN [10]
RP MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR
RP CLUSTERS.
RX PubMed=8388253; DOI=10.1021/bi00070a018;
RA Augier V., Asso M., Guigliarelli B., More C., Bertrand P., Santini C.-L.,
RA Blasco F., Chippaux M., Giordano G.;
RT "Removal of the high-potential [4Fe-4S] center of the beta-subunit from
RT Escherichia coli nitrate reductase. Physiological, biochemical, and EPR
RT characterization of site-directed mutated enzymes.";
RL Biochemistry 32:5099-5108(1993).
RN [11]
RP MUTAGENESIS OF CYSTEINE RESIDUES, AND EPR SPECTROSCOPY OF IRON-SULFUR
RP CLUSTERS.
RX PubMed=8664273; DOI=10.1021/bi952459p;
RA Guigliarelli B., Magalon A., Asso M., Bertrand P., Frixon C., Giordano G.,
RA Blasco F.;
RT "Complete coordination of the four Fe-S centers of the beta subunit from
RT Escherichia coli nitrate reductase. Physiological, biochemical, and EPR
RT characterization of site-directed mutants lacking the highest or lowest
RT potential [4Fe-4S] clusters.";
RL Biochemistry 35:4828-4836(1996).
RN [12]
RP EPR SPECTROSCOPY, AND REDOX POTENTIOMETRY OF IRON-SULFUR CLUSTERS.
RX PubMed=9516445; DOI=10.1074/jbc.273.13.7462;
RA Rothery R.A., Magalon A., Giordano G., Guigliarelli B., Blasco F.,
RA Weiner J.H.;
RT "The molybdenum cofactor of Escherichia coli nitrate reductase A (NarGHI).
RT Effect of a mobAB mutation and interactions with [Fe-S] clusters.";
RL J. Biol. Chem. 273:7462-7469(1998).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S)
RP AND IRON-SULFUR (4FE-4S), COFACTOR, AND SUBUNIT.
RX PubMed=12910261; DOI=10.1038/nsb969;
RA Bertero M.G., Rothery R.A., Palak M., Hou C., Lim D., Blasco F.,
RA Weiner J.H., Strynadka N.C.J.;
RT "Insights into the respiratory electron transfer pathway from the structure
RT of nitrate reductase A.";
RL Nat. Struct. Biol. 10:681-687(2003).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S)
RP AND IRON-SULFUR (4FE-4S), AND COFACTOR.
RX PubMed=14725769; DOI=10.1016/j.str.2003.11.020;
RA Jormakka M., Richardson D., Byrne B., Iwata S.;
RT "Architecture of NarGH reveals a structural classification of Mo-bisMGD
RT enzymes.";
RL Structure 12:95-104(2004).
CC -!- FUNCTION: The nitrate reductase enzyme complex allows E.coli to use
CC nitrate as an electron acceptor during anaerobic growth. The beta chain
CC is an electron transfer unit containing four cysteine clusters involved
CC in the formation of iron-sulfur centers. Electrons are transferred from
CC the gamma chain to the molybdenum cofactor of the alpha subunit.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinol + nitrate = a quinone + H2O + nitrite;
CC Xref=Rhea:RHEA:56144, ChEBI:CHEBI:15377, ChEBI:CHEBI:16301,
CC ChEBI:CHEBI:17632, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.7.5.1;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769};
CC Note=Binds 3 [4Fe-4S] clusters per subunit.
CC {ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769};
CC Note=Binds 1 [3Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:12910261, ECO:0000269|PubMed:14725769};
CC -!- SUBUNIT: Dimer of heterotrimers each composed of an alpha, a beta and a
CC gamma chain. Alpha and beta are catalytic chains; gamma chains are
CC involved in binding the enzyme complex to the cytoplasmic membrane.
CC {ECO:0000269|PubMed:12910261}.
CC -!- INTERACTION:
CC P11349; P42593: fadH; NbExp=3; IntAct=EBI-555067, EBI-561933;
CC P11349; P09152: narG; NbExp=13; IntAct=EBI-555067, EBI-547248;
CC P11349; P19317: narW; NbExp=3; IntAct=EBI-555067, EBI-555088;
CC P11349; P19318: narY; NbExp=3; IntAct=EBI-555067, EBI-555059;
CC P11349; P19319: narZ; NbExp=6; IntAct=EBI-555067, EBI-547262;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC -!- INDUCTION: By nitrate.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/NAR/";
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DR EMBL; M20147; AAA24195.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74309.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36095.1; -; Genomic_DNA.
DR EMBL; X16181; CAA34304.1; -; Genomic_DNA.
DR PIR; F64869; RDECNB.
DR RefSeq; NP_415743.1; NC_000913.3.
DR RefSeq; WP_000702650.1; NZ_STEB01000023.1.
DR PDB; 1Q16; X-ray; 1.90 A; B=1-512.
DR PDB; 1R27; X-ray; 2.00 A; B/D=1-512.
DR PDB; 1SIW; X-ray; 2.20 A; B=1-512.
DR PDB; 1Y4Z; X-ray; 2.00 A; B=1-512.
DR PDB; 1Y5I; X-ray; 1.90 A; B=1-512.
DR PDB; 1Y5L; X-ray; 2.50 A; B=1-512.
DR PDB; 1Y5N; X-ray; 2.50 A; B=1-512.
DR PDB; 3EGW; X-ray; 1.90 A; B=1-509.
DR PDB; 3IR5; X-ray; 2.30 A; B=1-512.
DR PDB; 3IR6; X-ray; 2.80 A; B=1-512.
DR PDB; 3IR7; X-ray; 2.50 A; B=1-512.
DR PDBsum; 1Q16; -.
DR PDBsum; 1R27; -.
DR PDBsum; 1SIW; -.
DR PDBsum; 1Y4Z; -.
DR PDBsum; 1Y5I; -.
DR PDBsum; 1Y5L; -.
DR PDBsum; 1Y5N; -.
DR PDBsum; 3EGW; -.
DR PDBsum; 3IR5; -.
DR PDBsum; 3IR6; -.
DR PDBsum; 3IR7; -.
DR AlphaFoldDB; P11349; -.
DR SMR; P11349; -.
DR BioGRID; 4262231; 28.
DR BioGRID; 850147; 6.
DR ComplexPortal; CPX-1974; Nitrate reductase A complex.
DR DIP; DIP-10312N; -.
DR IntAct; P11349; 15.
DR STRING; 511145.b1225; -.
DR DrugBank; DB07349; (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE.
DR DrugBank; DB04464; N-Formylmethionine.
DR TCDB; 5.A.3.1.1; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P11349; -.
DR PaxDb; P11349; -.
DR PRIDE; P11349; -.
DR EnsemblBacteria; AAC74309; AAC74309; b1225.
DR EnsemblBacteria; BAA36095; BAA36095; BAA36095.
DR GeneID; 58390546; -.
DR GeneID; 945780; -.
DR KEGG; ecj:JW1216; -.
DR KEGG; eco:b1225; -.
DR PATRIC; fig|1411691.4.peg.1056; -.
DR EchoBASE; EB0633; -.
DR eggNOG; COG1140; Bacteria.
DR HOGENOM; CLU_043374_5_2_6; -.
DR InParanoid; P11349; -.
DR OMA; VYFNWQT; -.
DR PhylomeDB; P11349; -.
DR BioCyc; EcoCyc:NARH-MON; -.
DR BioCyc; MetaCyc:NARH-MON; -.
DR BRENDA; 1.7.5.1; 2026.
DR EvolutionaryTrace; P11349; -.
DR PRO; PR:P11349; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031224; C:intrinsic component of membrane; IDA:EcoCyc.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0044799; C:NarGHI complex; IDA:EcoCyc.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008940; F:nitrate reductase activity; IMP:EcoCyc.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR GO; GO:0042126; P:nitrate metabolic process; IDA:ComplexPortal.
DR CDD; cd10557; NarH_beta-like; 1.
DR Gene3D; 1.10.3650.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR029263; Nitr_red_bet_C.
DR InterPro; IPR038262; Nitr_red_bet_C_sf.
DR InterPro; IPR006547; NO3_Rdtase_bsu.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF14711; Nitr_red_bet_C; 1.
DR TIGRFAMs; TIGR01660; narH; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; 3Fe-4S; 4Fe-4S; Cell membrane; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Nitrate assimilation; Oxidoreductase; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..512
FT /note="Respiratory nitrate reductase 1 beta chain"
FT /id="PRO_0000096720"
FT DOMAIN 7..35
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 175..206
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 208..237
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 184
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 192
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 196
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 217
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 223
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 227
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 244
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 247
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 259
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12910261,
FT ECO:0000269|PubMed:14725769"
FT CONFLICT 398..417
FT /note="DTKPVLRALKRMLAMRHYKR -> EYQTGTARTETYAGDASLQT (in
FT Ref. 6; AAA24195)"
FT /evidence="ECO:0000305"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 51..57
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 142..148
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 329..334
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:1Q16"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 387..394
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 399..420
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 437..447
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:1Q16"
FT TURN 463..466
FT /evidence="ECO:0007829|PDB:1Q16"
FT HELIX 469..475
FT /evidence="ECO:0007829|PDB:1Q16"
SQ SEQUENCE 512 AA; 58066 MW; 2E7719C8D078BAEA CRC64;
MKIRSQVGMV LNLDKCIGCH TCSVTCKNVW TSREGVEYAW FNNVETKPGQ GFPTDWENQE
KYKGGWIRKI NGKLQPRMGN RAMLLGKIFA NPHLPGIDDY YEPFDFDYQN LHTAPEGSKS
QPIARPRSLI TGERMAKIEK GPNWEDDLGG EFDKLAKDKN FDNIQKAMYS QFENTFMMYL
PRLCEHCLNP ACVATCPSGA IYKREEDGIV LIDQDKCRGW RMCITGCPYK KIYFNWKSGK
SEKCIFCYPR IEAGQPTVCS ETCVGRIRYL GVLLYDADAI ERAASTENEK DLYQRQLDVF
LDPNDPKVIE QAIKDGIPLS VIEAAQQSPV YKMAMEWKLA LPLHPEYRTL PMVWYVPPLS
PIQSAADAGE LGSNGILPDV ESLRIPVQYL ANLLTAGDTK PVLRALKRML AMRHYKRAET
VDGKVDTRAL EEVGLTEAQA QEMYRYLAIA NYEDRFVVPS SHRELAREAF PEKNGCGFTF
GDGCHGSDTK FNLFNSRRID AIDVTSKTEP HP
