NAPA_CUPNH
ID NAPA_CUPNH Reviewed; 831 AA.
AC P39185; Q7WXC3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE EC=1.9.6.1 {ECO:0000255|HAMAP-Rule:MF_01630};
DE Flags: Precursor;
GN Name=napA {ECO:0000255|HAMAP-Rule:MF_01630, ECO:0000303|PubMed:8376334};
GN OrderedLocusNames=PHG211;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-50, FUNCTION,
RP CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=8376334; DOI=10.1128/jb.175.18.5867-5876.1993;
RA Siddiqui R.A., Warnecke-Eberz U., Hengsberger A., Schneider B., Kostka S.,
RA Friedrich B.;
RT "Structure and function of a periplasmic nitrate reductase in Alcaligenes
RT eutrophus H16.";
RL J. Bacteriol. 175:5867-5876(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
RN [3] {ECO:0007744|PDB:3ML1, ECO:0007744|PDB:3O5A}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 30-831 IN COMPLEX WITH
RP IRON-SULFUR (4FE-4S) AND MOLYBDENUM MOLYBDOPTERIN COFACTOR, COFACTOR, AND
RP SUBUNIT.
RX PubMed=21419779; DOI=10.1016/j.jmb.2011.03.016;
RA Coelho C., Gonzalez P.J., Moura J.G., Moura I., Trincao J., Joao Romao M.;
RT "The crystal structure of Cupriavidus necator nitrate reductase in oxidized
RT and partially reduced states.";
RL J. Mol. Biol. 408:932-948(2011).
CC -!- FUNCTION: Catalytic subunit of the periplasmic nitrate reductase
CC complex NapAB. Receives electrons from NapB and catalyzes the reduction
CC of nitrate to nitrite. {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:8376334}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(II)-[cytochrome] + 2 H(+) + nitrate = 2 Fe(III)-
CC [cytochrome] + H2O + nitrite; Xref=Rhea:RHEA:12909, Rhea:RHEA-
CC COMP:11777, Rhea:RHEA-COMP:11778, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.9.6.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:8376334};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:21419779};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:21419779};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:21419779};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:21419779};
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:21419779, ECO:0000269|PubMed:8376334}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000305|PubMed:8376334}.
CC -!- INDUCTION: Expressed independently of nitrate induction and
CC anaerobiosis.
CC -!- PTM: Predicted to be exported by the Tat system (By similarity). The
CC position of the signal peptide cleavage has been experimentally proven
CC (PubMed:8376334). {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:8376334}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. NasA/NapA/NarB subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01630}.
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DR EMBL; X71385; CAA50507.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP85963.1; -; Genomic_DNA.
DR PIR; A48489; A48489.
DR RefSeq; WP_011154126.1; NZ_CP039289.1.
DR PDB; 3ML1; X-ray; 1.60 A; A=30-831.
DR PDB; 3O5A; X-ray; 1.72 A; A=30-831.
DR PDBsum; 3ML1; -.
DR PDBsum; 3O5A; -.
DR AlphaFoldDB; P39185; -.
DR SMR; P39185; -.
DR STRING; 381666.PHG211; -.
DR EnsemblBacteria; AAP85963; AAP85963; PHG211.
DR GeneID; 39976666; -.
DR KEGG; reh:PHG211; -.
DR PATRIC; fig|381666.6.peg.159; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_4; -.
DR OMA; GMNAHQH; -.
DR OrthoDB; 323168at2; -.
DR BRENDA; 1.9.6.1; 231.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0050140; F:nitrate reductase (cytochrome) activity; IEA:UniProtKB-EC.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd02791; MopB_CT_Nitrate-R-NapA-like; 1.
DR HAMAP; MF_01630; Nitrate_reduct_NapA; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041957; CT_Nitrate-R-NapA-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR010051; Periplasm_NO3_reductase_lsu.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01706; NAPA; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Molybdenum; Nitrate assimilation;
KW Oxidoreductase; Periplasm; Plasmid; Reference proteome; Signal; Transport.
FT SIGNAL 1..29
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:8376334"
FT CHAIN 30..831
FT /note="Periplasmic nitrate reductase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT /id="PRO_0000019168"
FT DOMAIN 41..97
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 83
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 85
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 152
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 177
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 181
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 214..221
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 245..249
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 264..266
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 375
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 379
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 485
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 511..512
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 534
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 561
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 721..730
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 797
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT BINDING 805
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT BINDING 822
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630,
FT ECO:0000269|PubMed:21419779, ECO:0007744|PDB:3ML1,
FT ECO:0007744|PDB:3O5A"
FT CONFLICT 146..151
FT /note="GMFGSG -> ACSAPA (in Ref. 1; CAA50507)"
FT /evidence="ECO:0000305"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:3ML1"
FT TURN 76..80
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 122..139
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:3ML1"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 202..206
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:3ML1"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 341..348
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 352..363
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 383..397
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:3ML1"
FT TURN 414..419
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 439..448
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 464..472
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:3ML1"
FT TURN 493..496
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 497..502
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 523..529
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 543..548
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 561..569
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 580..583
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 594..598
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 619..624
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 628..640
FT /evidence="ECO:0007829|PDB:3ML1"
FT TURN 641..644
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 650..655
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 659..662
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 670..674
FT /evidence="ECO:0007829|PDB:3ML1"
FT TURN 675..677
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 697..701
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 717..722
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 734..736
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 738..743
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 753..758
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 766..770
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 775..785
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 792..797
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 804..806
FT /evidence="ECO:0007829|PDB:3ML1"
FT TURN 814..816
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 824..830
FT /evidence="ECO:0007829|PDB:3ML1"
SQ SEQUENCE 831 AA; 93346 MW; 34CE1CDE6677C42F CRC64;
MKISRRDFIK QTAITATASV AGVTLPAGAA NFVTDSEVTK LKWSKAPCRF CGTGCGVTVA
VKDNKVVATQ GDPQAEVNKG LNCVKGYFLS KIMYGQDRLT RPLMRMKNGK YDKNGDFAPV
TWDQAFDEME RQFKRVLKEK GPTAVGMFGS GQWTVWEGYA AAKLYKAGFR SNNIDPNARH
CMASAAAGFM RTFGMDEPMG CYDDFEAADA FVLWGSNMAE MHPILWTRVT DRRLSHPKTR
VVVLSTFTHR CFDLADIGII FKPQTDLAML NYIANYIIRN NKVNKDFVNK HTVFKEGVTD
IGYGLRPDHP LQKAAKNASD PGAAKVITFD EFAKFVSKYD ADYVSKLSAV PKAKLDQLAE
LYADPNIKVM SLWTMGFNQH TRGTWANNMV YNLHLLTGKI ATPGNSPFSL TGQPSACGTA
REVGTFSHRL PADMVVTNPK HREEAERIWK LPPGTIPDKP GYDAVLQNRM LKDGKLNAYW
VQVNNNMQAA ANLMEEGLPG YRNPANFIVV SDAYPTVTAL AADLVLPSAM WVEKEGAYGN
AERRTQFWHQ LVDAPGEARS DLWQLVEFAK RFKVEEVWPP ELIAKKPEYK GKTLYDVLYR
NGQVDKFPLK DVNAEYHNAE AKAFGFYLQK GLFEEYATFG RGHGHDLAPF DAYHEARGLR
WPVVNGKETR WRYREGSDPY VKAGTGFQFY GNPDGKAVIF ALPYEPPAES PDKEYPYWLV
TGRVLEHWHS GSMTRRVPEL YRSFPNAVVF MHPEDAKALG LRRGVEVEVV SRRGRMRSRI
ETRGRDAPPR GLVFVPWFDA SQLINKVTLD ATCPISLQTD FKKCAVKIVK V
