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 24-JAN-2024, entry version 144. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7MCI; X-ray; 1.65 A; A/C=1-492. DR PDB; 7UT6; EM; 1.91 A; A/C=1-492. DR PDB; 7UT7; EM; 1.91 A; A/C=1-492. DR PDB; 7UT8; EM; 2.43 A; A/C=1-492. DR PDB; 7UT9; EM; 2.44 A; A/C=1-492. DR PDB; 7UTA; EM; 2.40 A; A/C=1-492. DR PDB; 8CRS; EM; 2.04 A; A/C=1-480. DR PDB; 8DBX; EM; 1.92 A; A/C=1-492. DR PDB; 8DBY; EM; 2.26 A; A/C=1-492. DR PDB; 8DFC; EM; 2.48 A; A/C=1-492. DR PDB; 8DFD; EM; 2.12 A; A/C=1-492. DR PDB; 8DPN; EM; 2.49 A; A/C=1-492. DR PDB; 8E3T; X-ray; 2.20 A; A/C=1-492. DR PDB; 8E3U; X-ray; 1.99 A; A/C=1-492. DR PDB; 8E3V; X-ray; 2.00 A; A/C=1-492. DR PDB; 8ENL; EM; 2.37 A; A/C=4-480. DR PDB; 8ENM; EM; 2.14 A; A/C=1-492. DR PDB; 8ENN; EM; 2.58 A; A/C=4-480. DR PDB; 8ENO; EM; 2.71 A; A/C=4-480. 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 PDBsum; 7MCI; -. DR PDBsum; 7UT6; -. DR PDBsum; 7UT7; -. DR PDBsum; 7UT8; -. DR PDBsum; 7UT9; -. DR PDBsum; 7UTA; -. DR PDBsum; 8CRS; -. DR PDBsum; 8DBX; -. DR PDBsum; 8DBY; -. DR PDBsum; 8DFC; -. DR PDBsum; 8DFD; -. DR PDBsum; 8DPN; -. DR PDBsum; 8E3T; -. DR PDBsum; 8E3U; -. DR PDBsum; 8E3V; -. DR PDBsum; 8ENL; -. DR PDBsum; 8ENM; -. DR PDBsum; 8ENN; -. DR PDBsum; 8ENO; -. DR AlphaFoldDB; P07328; -. DR EMDB; EMD-26756; -. DR EMDB; EMD-26757; -. DR EMDB; EMD-26760; -. DR EMDB; EMD-26763; -. DR EMDB; EMD-26764; -. DR EMDB; EMD-26957; -. DR EMDB; EMD-27316; -. DR EMDB; EMD-27317; -. DR EMDB; EMD-27404; -. DR EMDB; EMD-27405; -. DR EMDB; EMD-27639; -. DR EMDB; EMD-28272; -. DR EMDB; EMD-28273; -. DR SMR; P07328; -. DR DIP; DIP-6252N; -. DR BioCyc; MetaCyc:MONOMER-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 Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3. 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 NCBIfam; TIGR01862; N2-ase-Ialpha; 1. DR NCBIfam; TIGR01282; nifD; 1. DR PANTHER; PTHR43457; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1. DR PANTHER; PTHR43457:SF1; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1. DR Pfam; PF00148; Oxidored_nitro; 1. DR SUPFAM; SSF53807; Helical backbone' metal receptor; 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 //