NIFD_AZOVI
ID NIFD_AZOVI Reviewed; 492 AA.
AC P07328;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Nitrogenase molybdenum-iron protein alpha chain;
DE EC=1.18.6.1;
DE AltName: Full=Dinitrogenase;
DE AltName: Full=Nitrogenase component I;
GN Name=nifD;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=2644218; DOI=10.1128/jb.171.2.1017-1027.1989;
RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S.,
RA Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT "Physical and genetic map of the major nif gene cluster from Azotobacter
RT vinelandii.";
RL J. Bacteriol. 171:1017-1027(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-409.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=3344210; DOI=10.1093/nar/16.3.1207;
RA Hiratsuka K., Roy K.L.;
RT "Sequence of a 1.4 kb Eco RI fragment of Azotobacter vinelandii nif DNA.";
RL Nucleic Acids Res. 16:1207-1207(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=3863780; DOI=10.1016/0378-1119(85)90255-0;
RA Brigle K.E., Newton W.E., Dean D.R.;
RT "Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase
RT structural gene cluster.";
RL Gene 37:37-44(1985).
RN [4]
RP PROTEIN SEQUENCE OF 2-20.
RX PubMed=649581; DOI=10.1016/s0021-9258(17)34817-2;
RA Lundell D.J., Howard J.B.;
RT "Isolation and partial characterization of two different subunits from the
RT molybdenum-iron protein of Azotobacter vinelandii nitrogenase.";
RL J. Biol. Chem. 253:3422-3426(1978).
RN [5]
RP ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=CA;
RX PubMed=7830548; DOI=10.1111/j.1365-2958.1994.tb01270.x;
RA Moshiri F., Kim J.W., Fu C., Maier R.J.;
RT "The FeSII protein of Azotobacter vinelandii is not essential for aerobic
RT nitrogen fixation, but confers significant protection to oxygen-mediated
RT inactivation of nitrogenase in vitro and in vivo.";
RL Mol. Microbiol. 14:101-114(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RA Kim J., Rees D.C.;
RT "Crystallographic structure and functional implications of the nitrogenase
RT molybdenum-iron protein from Azotobacter vinelandii.";
RL Nature 360:553-560(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH FE(8)-S(7) CLUSTER
RP AND IRON-SULFUR-MOLYBDENUM CLUSTER, SUBUNIT, AND COFACTOR.
RX PubMed=9163420; DOI=10.1038/387370a0;
RA Schindelin H., Kisker C., Schlessman J.L., Howard J.B., Rees D.C.;
RT "Structure of ADP x [AlF(4)](-)-stabilized nitrogenase complex and its
RT implications for signal transduction.";
RL Nature 387:370-376(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FE(8)-S(7) CLUSTER
RP AND IRON-SULFUR-MOLYBDENUM CLUSTER, SUBUNIT, AND COFACTOR.
RX PubMed=9063865; DOI=10.1021/bi9626665;
RA Peters J.W., Stowell M.H.B., Soltis S.M., Finnegan M.G., Johnson M.K.,
RA Rees D.C.;
RT "Redox-dependent structural changes in the nitrogenase P-cluster.";
RL Biochemistry 36:1181-1187(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH FE(8)-S(7) CLUSTER
RP AND IRON-SULFUR-MOLYBDENUM CLUSTER, SUBUNIT, AND COFACTOR.
RX PubMed=11170380; DOI=10.1021/bi001645e;
RA Chiu H.-J., Peters J.W., Lanzilotta W.N., Ryle M.J., Seefeldt L.C.,
RA Howard J.B., Rees D.C.;
RT "MgATP-bound and nucleotide-free structures of a nitrogenase protein
RT complex between the Leu 127Delta-Fe-protein and the MoFe-protein.";
RL Biochemistry 40:641-650(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLN-195 IN COMPLEX WITH
RP IRON-SULFUR-MOLYBDENUM CLUSTER, SUBUNIT, AND COFACTOR.
RX PubMed=11327812; DOI=10.1021/bi0013997;
RA Soerlie M., Christiansen J., Lemon B.J., Peters J.W., Dean D.R.,
RA Hales B.J.;
RT "Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe
RT protein.";
RL Biochemistry 40:1540-1549(2001).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF CROSS-LINKED HETERODIMER WITH
RP FE-PROTEIN IN COMPLEX WITH FE(8)-S(7) CLUSTER AND IRON-SULFUR-MOLYBDENUM
RP CLUSTER, SUBUNIT, AND COFACTOR.
RX PubMed=12501184; DOI=10.1021/bi026642b;
RA Schmid B., Einsle O., Chiu H.J., Willing A., Yoshida M., Howard J.B.,
RA Rees D.C.;
RT "Biochemical and structural characterization of the cross-linked complex of
RT nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure.";
RL Biochemistry 41:15557-15565(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=11951047; DOI=10.1126/science.1070010;
RA Schmid B., Ribbe M.W., Einsle O., Yoshida M., Thomas L.M., Dean D.R.,
RA Rees D.C., Burgess B.K.;
RT "Structure of a cofactor-deficient nitrogenase MoFe protein.";
RL Science 296:352-356(2002).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS) IN COMPLEX WITH FE(7)-MO-S(9)-N
RP CLUSTER, SUBUNIT, AND COFACTOR.
RX PubMed=12215645; DOI=10.1126/science.1073877;
RA Einsle O., Tezcan F.A., Andrade S.L.A., Schmid B., Yoshida M., Howard J.B.,
RA Rees D.C.;
RT "Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the
RT FeMo-cofactor.";
RL Science 297:1696-1700(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FE(7)-MO-S(9)-N
RP CLUSTER AND FE(8)-S(7) CLUSTER, SUBUNIT, AND COFACTOR.
RX PubMed=16123301; DOI=10.1126/science.1115653;
RA Tezcan F.A., Kaiser J.T., Mustafi D., Walton M.Y., Howard J.B., Rees D.C.;
RT "Nitrogenase complexes: multiple docking sites for a nucleotide switch
RT protein.";
RL Science 309:1377-1380(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.00 ANGSTROMS) IN COMPLEX WITH FE(8)-S(7) CLUSTER
RP AND 7FE-MO-9S-C-HOMOCITRYL CLUSTER, COFACTOR, AND SUBUNIT.
RX PubMed=22096190; DOI=10.1126/science.1214025;
RA Spatzal T., Aksoyoglu M., Zhang L., Andrade S.L., Schleicher E., Weber S.,
RA Rees D.C., Einsle O.;
RT "Evidence for interstitial carbon in nitrogenase FeMo cofactor.";
RL Science 334:940-940(2011).
CC -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase
CC complex that catalyzes the key enzymatic reactions in nitrogen
CC fixation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16
CC ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16
CC phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997,
CC ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=1.18.6.1;
CC -!- COFACTOR:
CC Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143;
CC Note=Binds 1 [8Fe-7S] cluster per heterodimer.;
CC -!- COFACTOR:
CC Name=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409;
CC Note=Binds 1 [7Fe-Mo-9S-C-homocitryl] cluster per subunit.;
CC -!- ACTIVITY REGULATION: Nitrogenase holoenzyme is subject to
CC 'conformational protection' by FeSII; under oxidizing conditions FeSII
CC binds to the holoenzyme and reversibly protects it from oxidation
CC (PubMed:7830548). {ECO:0000269|PubMed:7830548}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC the iron protein (nitrogenase component 2).
CC {ECO:0000269|PubMed:11170380, ECO:0000269|PubMed:11327812,
CC ECO:0000269|PubMed:12215645, ECO:0000269|PubMed:12501184,
CC ECO:0000269|PubMed:16123301, ECO:0000269|PubMed:22096190,
CC ECO:0000269|PubMed:9063865, ECO:0000269|PubMed:9163420}.
CC -!- INDUCTION: Constitutively expressed during log and stationary phase in
CC sucrose-limited cultures, its levels decrease during stationary phase
CC (at protein level). {ECO:0000269|PubMed:7830548}.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR EMBL; M20568; AAA64710.1; -; Genomic_DNA.
DR EMBL; M11579; AAA22143.1; -; Genomic_DNA.
DR EMBL; X06886; CAA30004.1; -; Genomic_DNA.
DR PIR; A43049; NIAVMA.
DR RefSeq; WP_012698832.1; NZ_FPKM01000020.1.
DR PDB; 1FP4; X-ray; 2.50 A; A/C=1-492.
DR PDB; 1G20; X-ray; 2.20 A; A/C=1-492.
DR PDB; 1G21; X-ray; 3.00 A; A/C=1-492.
DR PDB; 1L5H; X-ray; 2.30 A; A=2-492.
DR PDB; 1M1N; X-ray; 1.16 A; A/C/E/G=2-492.
DR PDB; 1M1Y; X-ray; 3.20 A; A/C/I/K=2-492.
DR PDB; 1M34; X-ray; 2.30 A; A/C/I/K=2-492.
DR PDB; 1N2C; X-ray; 3.00 A; A/C=2-492.
DR PDB; 2AFH; X-ray; 2.10 A; A/C=2-492.
DR PDB; 2AFI; X-ray; 3.10 A; A/C/I/K=2-492.
DR PDB; 2MIN; X-ray; 2.03 A; A/C=2-492.
DR PDB; 3K1A; X-ray; 2.23 A; A/C=2-492.
DR PDB; 3MIN; X-ray; 2.03 A; A/C=2-492.
DR PDB; 3U7Q; X-ray; 1.00 A; A/C=1-492.
DR PDB; 4ND8; X-ray; 2.00 A; A/C=1-492.
DR PDB; 4TKU; X-ray; 1.43 A; A/C=1-492.
DR PDB; 4TKV; X-ray; 1.50 A; A/C=1-492.
DR PDB; 4WNA; X-ray; 2.00 A; A/C=1-492.
DR PDB; 4WZA; X-ray; 1.90 A; A/C=4-480.
DR PDB; 4WZB; X-ray; 2.30 A; A/C=4-480.
DR PDB; 4XPI; X-ray; 1.97 A; A/C=3-492.
DR PDB; 5BVG; X-ray; 1.60 A; A/C=1-492.
DR PDB; 5BVH; X-ray; 1.53 A; A/C=1-492.
DR PDB; 5CX1; X-ray; 1.75 A; A/C/E/G/I/K/M/O=1-480.
DR PDB; 5VQ4; X-ray; 2.30 A; A/C=1-492.
DR PDB; 6BBL; X-ray; 1.68 A; A/C=1-492.
DR PDB; 6CDK; X-ray; 2.10 A; A/C=1-492.
DR PDB; 6O7L; X-ray; 2.26 A; A/C=1-492.
DR PDB; 6O7M; X-ray; 1.40 A; A/C=1-492.
DR PDB; 6O7N; X-ray; 1.75 A; A/C=1-492.
DR PDB; 6O7O; X-ray; 1.89 A; A/C=1-492.
DR PDB; 6O7P; X-ray; 1.70 A; A/C=1-492.
DR PDB; 6O7Q; X-ray; 2.00 A; A/C=1-492.
DR PDB; 6O7R; X-ray; 2.27 A; A/C=1-492.
DR PDB; 6O7S; X-ray; 2.27 A; A/C=1-492.
DR PDB; 6OP1; X-ray; 1.70 A; A/C=4-480.
DR PDB; 6OP2; X-ray; 1.90 A; A/C=4-480.
DR PDB; 6OP3; X-ray; 1.60 A; A/C=4-480.
DR PDB; 6OP4; X-ray; 2.30 A; A/C=4-480.
DR PDB; 6UG0; X-ray; 1.83 A; A/C=1-492.
DR PDB; 6VXT; X-ray; 1.74 A; A/C=1-492.
DR PDB; 7JRF; X-ray; 1.33 A; A/C=1-492.
DR PDBsum; 1FP4; -.
DR PDBsum; 1G20; -.
DR PDBsum; 1G21; -.
DR PDBsum; 1L5H; -.
DR PDBsum; 1M1N; -.
DR PDBsum; 1M1Y; -.
DR PDBsum; 1M34; -.
DR PDBsum; 1N2C; -.
DR PDBsum; 2AFH; -.
DR PDBsum; 2AFI; -.
DR PDBsum; 2MIN; -.
DR PDBsum; 3K1A; -.
DR PDBsum; 3MIN; -.
DR PDBsum; 3U7Q; -.
DR PDBsum; 4ND8; -.
DR PDBsum; 4TKU; -.
DR PDBsum; 4TKV; -.
DR PDBsum; 4WNA; -.
DR PDBsum; 4WZA; -.
DR PDBsum; 4WZB; -.
DR PDBsum; 4XPI; -.
DR PDBsum; 5BVG; -.
DR PDBsum; 5BVH; -.
DR PDBsum; 5CX1; -.
DR PDBsum; 5VQ4; -.
DR PDBsum; 6BBL; -.
DR PDBsum; 6CDK; -.
DR PDBsum; 6O7L; -.
DR PDBsum; 6O7M; -.
DR PDBsum; 6O7N; -.
DR PDBsum; 6O7O; -.
DR PDBsum; 6O7P; -.
DR PDBsum; 6O7Q; -.
DR PDBsum; 6O7R; -.
DR PDBsum; 6O7S; -.
DR PDBsum; 6OP1; -.
DR PDBsum; 6OP2; -.
DR PDBsum; 6OP3; -.
DR PDBsum; 6OP4; -.
DR PDBsum; 6UG0; -.
DR PDBsum; 6VXT; -.
DR PDBsum; 7JRF; -.
DR AlphaFoldDB; P07328; -.
DR SMR; P07328; -.
DR DIP; DIP-6252N; -.
DR BioCyc; MetaCyc:MON-19493; -.
DR BRENDA; 1.18.6.1; 49.
DR EvolutionaryTrace; P07328; -.
DR GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR CDD; cd01976; Nitrogenase_MoFe_alpha; 1.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR010143; Nase_comp1_asu.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR005972; Nase_Mo-Fe_asu.
DR PANTHER; PTHR43457; PTHR43457; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR TIGRFAMs; TIGR01862; N2-ase-Ialpha; 1.
DR TIGRFAMs; TIGR01282; nifD; 1.
DR PROSITE; PS00699; NITROGENASE_1_1; 1.
DR PROSITE; PS00090; NITROGENASE_1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Molybdenum; Nitrogen fixation; Nucleotide-binding;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:649581"
FT CHAIN 2..492
FT /note="Nitrogenase molybdenum-iron protein alpha chain"
FT /id="PRO_0000153058"
FT BINDING 62
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT BINDING 88
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT BINDING 154
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT BINDING 275
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT BINDING 442
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT MUTAGEN 195
FT /note="H->Q: No nitrogenase activity."
FT CONFLICT 3
FT /note="G -> R (in Ref. 3; AAA22143)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="S -> C (in Ref. 3; AAA22143)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="E -> A (in Ref. 3; AAA22143)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..261
FT /note="SISE -> YISQ (in Ref. 3; AAA22143)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="Y -> M (in Ref. 3; AAA22143)"
FT /evidence="ECO:0000305"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:3U7Q"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3U7Q"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1M1Y"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:3U7Q"
FT TURN 206..212
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:3U7Q"
FT TURN 232..235
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 302..313
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 318..346
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:3U7Q"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 373..381
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 384..391
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 406..416
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 425..433
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 452..467
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:2MIN"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:4XPI"
SQ SEQUENCE 492 AA; 55289 MW; 7D4B2CF5E99664D7 CRC64;
MTGMSREEVE SLIQEVLEVY PEKARKDRNK HLAVNDPAVT QSKKCIISNK KSQPGLMTIR
GCAYAGSKGV VWGPIKDMIH ISHGPVGCGQ YSRAGRRNYY IGTTGVNAFV TMNFTSDFQE
KDIVFGGDKK LAKLIDEVET LFPLNKGISV QSECPIGLIG DDIESVSKVK GAELSKTIVP
VRCEGFRGVS QSLGHHIAND AVRDWVLGKR DEDTTFASTP YDVAIIGDYN IGGDAWSSRI
LLEEMGLRCV AQWSGDGSIS EIELTPKVKL NLVHCYRSMN YISRHMEEKY GIPWMEYNFF
GPTKTIESLR AIAAKFDESI QKKCEEVIAK YKPEWEAVVA KYRPRLEGKR VMLYIGGLRP
RHVIGAYEDL GMEVVGTGYE FAHNDDYDRT MKEMGDSTLL YDDVTGYEFE EFVKRIKPDL
IGSGIKEKFI FQKMGIPFRE MHSWDYSGPY HGFDGFAIFA RDMDMTLNNP CWKKLQAPWE
ASEGAEKVAA SA
