ID NAPA_CERS4 Reviewed; 831 AA.
AC Q53176; Q3IV43;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 27-MAR-2024, entry version 158.
DE RecName: Full=Periplasmic nitrate reductase {ECO:0000255|HAMAP-Rule:MF_01630};
DE EC=1.9.6.1 {ECO:0000255|HAMAP-Rule:MF_01630, ECO:0000269|PubMed:14528294};
DE Flags: Precursor;
GN Name=napA {ECO:0000255|HAMAP-Rule:MF_01630}; OrderedLocusNames=RHOS4_40230;
GN ORFNames=RSP_4116;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OG Plasmid pRS241c.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8730872; DOI=10.1111/j.1365-2958.1996.tb02475.x;
RA Reyes F., Roldan M.D., Klipp W., Castillo F., Moreno-Vivian C.;
RT "Isolation of periplasmic nitrate reductase genes from Rhodobacter
RT sphaeroides DSM 158: structural and functional differences among
RT prokaryotic nitrate reductases.";
RL Mol. Microbiol. 19:1307-1318(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.; PLASMID=pRS241c;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of plasmid C of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 30-831 IN COMPLEX WITH NAPB;
RP IRON-SULFUR (4FE-4S) AND MOLYBDENUM MOLYBDOPTERIN COFACTOR, CATALYTIC
RP ACTIVITY, AND COFACTOR.
RX PubMed=14528294; DOI=10.1038/nsb994;
RA Arnoux P., Sabaty M., Alric J., Frangioni B., Guigliarelli B.,
RA Adriano J.-M., Pignol D.;
RT "Structural and redox plasticity in the heterodimeric periplasmic nitrate
RT reductase.";
RL Nat. Struct. Biol. 10:928-934(2003).
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:14528294}.
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:14528294};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:14528294};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01630,
CC ECO:0000269|PubMed:14528294};
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:14528294};
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:14528294};
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:14528294}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01630}.
CC -!- INDUCTION: Nitrate reductase activity can be induced by nitrate and not
CC repressed by ammonium or oxygen.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|HAMAP-Rule:MF_01630}.
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; Z46806; CAA86827.1; -; Genomic_DNA.
DR EMBL; CP000146; ABA81591.1; -; Genomic_DNA.
DR RefSeq; WP_011331398.1; NZ_CP030275.1.
DR RefSeq; YP_345332.1; NC_007489.1.
DR PDB; 1OGY; X-ray; 3.20 A; A/C/E/G/I/K/M/O=30-831.
DR PDBsum; 1OGY; -.
DR AlphaFoldDB; Q53176; -.
DR SMR; Q53176; -.
DR IntAct; Q53176; 1.
DR EnsemblBacteria; ABA81591; ABA81591; RSP_4116.
DR KEGG; rsp:RSP_4116; -.
DR PATRIC; fig|272943.9.peg.178; -.
DR OrthoDB; 9816402at2; -.
DR PhylomeDB; Q53176; -.
DR BRENDA; 1.9.6.1; 5383.
DR EvolutionaryTrace; Q53176; -.
DR Proteomes; UP000002703; Plasmid pRS241c.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:0045333; P:cellular respiration; IEA:UniProt.
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 CDD; cd02754; MopB_Nitrate-R-NapA-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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 NCBIfam; TIGR01706; NAPA; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43105:SF11; PERIPLASMIC NITRATE REDUCTASE; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
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; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 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; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Molybdenum; Nitrate assimilation; Oxidoreductase; Periplasm; Plasmid;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..29
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT CHAIN 30..831
FT /note="Periplasmic nitrate reductase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01630"
FT /id="PRO_0000019171"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
FT BINDING 245..249
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250|UniProtKB:P39185, ECO:0000255|HAMAP-
FT Rule:MF_01630"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
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:14528294, ECO:0007744|PDB:1OGY"
FT CONFLICT 135
FT /note="R -> L (in Ref. 1; CAA86827)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="G -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="K -> E (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="M -> S (in Ref. 1; CAA86827)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="A -> S (in Ref. 1; CAA86827)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="L -> R (in Ref. 1; CAA86827)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="V -> W (in Ref. 1; CAA86827)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="S -> F (in Ref. 1; CAA86827)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="C -> A (in Ref. 1; CAA86827)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="R -> H (in Ref. 1; CAA86827)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="V -> W (in Ref. 1; CAA86827)"
FT /evidence="ECO:0000305"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:1OGY"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 122..139
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 155..166
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 250..253
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:1OGY"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 285..291
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 329..337
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 341..348
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 369..374
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 383..397
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:1OGY"
FT TURN 414..419
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:1OGY"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 439..448
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 464..472
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:1OGY"
FT TURN 491..497
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 522..528
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 543..548
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 561..569
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 580..585
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:1OGY"
FT TURN 594..599
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 614..617
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 623..626
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 628..637
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 640..644
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 652..655
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 670..675
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 692..694
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 697..701
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 713..715
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 717..722
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 734..736
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 738..743
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 753..758
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 766..770
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 775..787
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 792..796
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 804..806
FT /evidence="ECO:0007829|PDB:1OGY"
FT TURN 814..816
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 825..829
FT /evidence="ECO:0007829|PDB:1OGY"
SQ SEQUENCE 831 AA; 92637 MW; 74B35640749CC906 CRC64;
MTLTRRDLIK AQAAATAAAA AGLPVSALAQ PVTGGAEALR IRWSKAPCRF CGTGCGVMVG
TRDGQVVATH GDTQAEVNRG LNCVKGYFLS KIMYGEDRLT TPLLRMKDGV YHKEGEFAPV
SWDEAFDVMA AQAKRVLKEK GPKAVGMFGS GQWTIWEGYA ASKLMRAGFR SNNLDPNARH
CMASAATAFM RTFGMDEPMG CYDDFEAADA FVLWGSNMAE MHPILWSRLT DRRLSHEHVR
VAVLSTFTHR SMDLADTPII FRPGTDLAIL NYIAHHIIST GRVNRDFVDR HTNFALGATD
IGYGLRPEHQ LQLAAKGAAD AGAMTPTDFE TFAALVSEYT LEKAAEISGV EPALLEELAE
LYADPDRKVM SLWTMGFNQH VRGVWANHMV YNLHLLTGKI SEPGNSPFSL TGQPSACGTA
REVGTFAHRL PADMVVTNPE HRAHAEEIWK LPAGLLPDWV GAHAVEQDRK LHDGEINFYW
VQVNNNMQAA PNIDQETYPG YRNPENFIVV SDAYPTVTGR CADLVLPAAM WVEKEGAYGN
AERRTHFWHQ LVEAPGEARS DLWQLMEFSK RFTTDEVWPE EILSAAPAYR GKTLFEVLFA
NGSVDRFPAS DVNPDHANHE AALFGFYPQK GLFEEYAAFG RGHGHDLAPF DTYHEVRGLR
WPVVEGEETR WRYREGFDPY VKPGEGLRFY GKPDGRAVIL GVPYEPPAES PDEEFGFWLV
TGRVLEHWHS GSMTLRVPEL YKAFPGAVCF MHPEDARSRG LNRGSEVRVI SRRGEIRTRL
ETRGRNRMPR GVVFVPWFDA SQLINKVTLD ANDPISRQTD FKKCAVKIEA V
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