ID DSTOR_RHOCA Reviewed; 823 AA.
AC Q52675; P72249;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Dimethyl sulfoxide/trimethylamine N-oxide reductase;
DE Short=DMSO reductase;
DE Short=DMSOR;
DE Short=Me2SO reductase;
DE Short=TMAOR;
DE EC=1.7.2.3;
DE EC=1.8.5.3;
DE Flags: Precursor;
GN Name=dorA;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 43-59, FUNCTION AS A
RP DIMETHYL SULFOXIDE REDUCTASE AND TRIMETHYLAMINE N-OXIDE REDUCTASE,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RC STRAIN=DSM 938 / 37b4;
RX PubMed=8856102; DOI=10.1016/0005-2728(96)00092-8;
RA Shaw A.L., Hanson G.R., McEwan A.G.;
RT "Cloning and sequence analysis of the dimethylsulfoxide reductase
RT structural gene from Rhodobacter capsulatus.";
RL Biochim. Biophys. Acta 1276:176-180(1996).
RN [2]
RP SEQUENCE REVISION.
RA Shaw A.L., McEwan A.G.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 43-71, AND MASS
RP SPECTROMETRY.
RC STRAIN=DSM 938 / 37b4;
RX PubMed=8890911; DOI=10.1006/jmbi.1996.0554;
RA Knaeblein J., Mann K., Ehlert S., Fonstein M., Huber R., Schneider F.;
RT "Isolation, cloning, sequence analysis and localization of the operon
RT encoding dimethyl sulfoxide/trimethylamine N-oxide reductase from
RT Rhodobacter capsulatus.";
RL J. Mol. Biol. 263:40-52(1996).
RN [4]
RP FUNCTION AS A DIMETHYL SULFOXIDE REDUCTASE AND TRIMETHYLAMINE N-OXIDE
RP REDUCTASE, COFACTOR, AND SUBUNIT.
RC STRAIN=DSM 938 / 37b4;
RX PubMed=2001248; DOI=10.1042/bj2740305;
RA McEwan A.G., Ferguson S.J., Jackson J.B.;
RT "Purification and properties of dimethyl sulphoxide reductase from
RT Rhodobacter capsulatus. A periplasmic molybdoenzyme.";
RL Biochem. J. 274:305-307(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 43-823 IN COMPLEX WITH
RP MOLYBDOPTERIN, AND COFACTOR.
RX PubMed=8890912; DOI=10.1006/jmbi.1996.0555;
RA Schneider F., Loewe J., Huber R., Schindelin H., Kisker C., Knaeblein J.;
RT "Crystal structure of dimethyl sulfoxide reductase from Rhodobacter
RT capsulatus at 1.88-A resolution.";
RL J. Mol. Biol. 263:53-69(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN.
RC STRAIN=H123;
RA McAlpine A.S., McEwan A.G., Shaw A.L., Bailey S.;
RT "Molybdenum active centre of DMSO reductase from Rhodobacter capsulatus:
RT crystal structure of the oxidised enzyme at 1.82-A resolution and the
RT dithionite-reduced enzyme at 2.8-A resolution.";
RL J. Biol. Inorg. Chem. 2:690-700(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN.
RX PubMed=9466935; DOI=10.1006/jmbi.1997.1513;
RA McAlpine A.S., McEwan A.G., Bailey S.;
RT "The high resolution crystal structure of DMSO reductase in complex with
RT DMSO.";
RL J. Mol. Biol. 275:613-623(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN, AND
RP SUBUNIT.
RX PubMed=10985771; DOI=10.1021/bi0000521;
RA Bray R.C., Adams B., Smith A.T., Bennett B., Bailey S.;
RT "Reversible dissociation of thiolate ligands from molybdenum in an enzyme
RT of the dimethyl sulfoxide reductase family.";
RL Biochemistry 39:11258-11269(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN.
RX PubMed=10835270; DOI=10.1006/jmbi.2000.3702;
RA Stewart L.J., Bailey S., Bennett B., Charnock J.M., Garner C.D.,
RA McAlpine A.S.;
RT "Dimethylsulfoxide reductase: an enzyme capable of catalysis with either
RT molybdenum or tungsten at the active site.";
RL J. Mol. Biol. 299:593-600(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MOLYBDOPTERIN, AND
RP SUBUNIT.
RX PubMed=11502174; DOI=10.1021/bi010559r;
RA Bray R.C., Adams B., Smith A.T., Richards R.L., Lowe D.J., Bailey S.;
RT "Reactions of dimethylsulfoxide reductase in the presence of dimethyl
RT sulfide and the structure of the dimethyl sulfide-modified enzyme.";
RL Biochemistry 40:9810-9820(2001).
CC -!- FUNCTION: Catalyzes the reduction of dimethyl sulfoxide (DMSO) and
CC trimethylamine N-oxide (TMAO) to dimethyl sulfide (DMS) and
CC trimethylamine, respectively. The terminal DMSO reductase can also use
CC various sulfoxides and N-oxide compounds as terminal electron acceptor
CC in addition to DMSO and TMAO. {ECO:0000269|PubMed:2001248,
CC ECO:0000269|PubMed:8856102}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a menaquinone + dimethyl sulfide + H2O = a menaquinol +
CC dimethyl sulfoxide; Xref=Rhea:RHEA:28494, Rhea:RHEA-COMP:9537,
CC Rhea:RHEA-COMP:9539, ChEBI:CHEBI:15377, ChEBI:CHEBI:16374,
CC ChEBI:CHEBI:17437, ChEBI:CHEBI:18151, ChEBI:CHEBI:28262; EC=1.8.5.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + trimethylamine = 2 Fe(II)-
CC [cytochrome c] + 3 H(+) + trimethylamine N-oxide;
CC Xref=Rhea:RHEA:24236, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15724,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58389; EC=1.7.2.3;
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Evidence={ECO:0000269|PubMed:2001248, ECO:0000269|PubMed:8890912};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:2001248,
CC ECO:0000269|PubMed:8890912};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10835270,
CC ECO:0000269|PubMed:10985771, ECO:0000269|PubMed:11502174,
CC ECO:0000269|PubMed:2001248, ECO:0000269|PubMed:8856102,
CC ECO:0000269|PubMed:8890912, ECO:0000269|PubMed:9466935,
CC ECO:0000269|Ref.6}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8856102}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- MASS SPECTROMETRY: Mass=86600; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:8890911};
CC -!- MASS SPECTROMETRY: Mass=85034; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8890911};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA64689.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U49506; AAD13674.1; -; Genomic_DNA.
DR EMBL; X95407; CAA64689.1; ALT_INIT; Genomic_DNA.
DR PDB; 1DMR; X-ray; 1.82 A; A=1-823.
DR PDB; 1DMS; X-ray; 1.88 A; A=43-823.
DR PDB; 1E18; X-ray; 2.00 A; A=1-823.
DR PDB; 1E5V; X-ray; 2.40 A; A/C=1-823.
DR PDB; 1E60; X-ray; 2.00 A; A/C=1-823.
DR PDB; 1E61; X-ray; 1.90 A; A/C=1-823.
DR PDB; 1H5N; X-ray; 2.00 A; A/C=1-823.
DR PDB; 2DMR; X-ray; 2.80 A; A=1-823.
DR PDB; 3DMR; X-ray; 2.50 A; A=1-823.
DR PDB; 4DMR; X-ray; 1.90 A; A=1-823.
DR PDBsum; 1DMR; -.
DR PDBsum; 1DMS; -.
DR PDBsum; 1E18; -.
DR PDBsum; 1E5V; -.
DR PDBsum; 1E60; -.
DR PDBsum; 1E61; -.
DR PDBsum; 1H5N; -.
DR PDBsum; 2DMR; -.
DR PDBsum; 3DMR; -.
DR PDBsum; 4DMR; -.
DR AlphaFoldDB; Q52675; -.
DR SMR; Q52675; -.
DR BRENDA; 1.8.5.3; 5381.
DR EvolutionaryTrace; Q52675; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR GO; GO:0009033; F:trimethylamine-N-oxide reductase activity; IEA:UniProtKB-EC.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR CDD; cd02769; MopB_DMSOR-BSOR-TMAOR; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006658; BisC.
DR InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR InterPro; IPR041460; Molybdopterin_N.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR00509; bisC_fam; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; Molybdenum;
KW Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..42
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:8856102, ECO:0000269|PubMed:8890911"
FT CHAIN 43..823
FT /note="Dimethyl sulfoxide/trimethylamine N-oxide reductase"
FT /id="PRO_0000019145"
FT BINDING 156..160
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 158
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:10835270,
FT ECO:0000269|PubMed:10985771, ECO:0000269|PubMed:11502174,
FT ECO:0000269|PubMed:8890912, ECO:0000269|PubMed:9466935,
FT ECO:0000269|Ref.6"
FT BINDING 189
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT BINDING 232..233
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 262..263
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 283..285
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 364..365
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 368
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:10835270,
FT ECO:0000269|PubMed:10985771, ECO:0000269|PubMed:11502174,
FT ECO:0000269|PubMed:8890912, ECO:0000269|PubMed:9466935,
FT ECO:0000269|Ref.6"
FT BINDING 476
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:10835270,
FT ECO:0000269|PubMed:10985771, ECO:0000269|PubMed:11502174,
FT ECO:0000269|PubMed:8890912, ECO:0000269|PubMed:9466935,
FT ECO:0000269|Ref.6"
FT BINDING 480
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:10835270,
FT ECO:0000269|PubMed:10985771, ECO:0000269|PubMed:11502174,
FT ECO:0000269|PubMed:8890912, ECO:0000269|PubMed:9466935,
FT ECO:0000269|Ref.6"
FT BINDING 500..501
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 523
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:10835270,
FT ECO:0000269|PubMed:10985771, ECO:0000269|PubMed:11502174,
FT ECO:0000269|PubMed:8890912, ECO:0000269|PubMed:9466935,
FT ECO:0000269|Ref.6"
FT BINDING 553
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:10835270,
FT ECO:0000269|PubMed:10985771, ECO:0000269|PubMed:11502174,
FT ECO:0000269|PubMed:8890912, ECO:0000269|PubMed:9466935,
FT ECO:0000269|Ref.6"
FT BINDING 685..686
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 691..693
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 779
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:10835270,
FT ECO:0000269|PubMed:10985771, ECO:0000269|PubMed:11502174,
FT ECO:0000269|PubMed:8890912, ECO:0000269|PubMed:9466935,
FT ECO:0000269|Ref.6"
FT BINDING 796..797
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT CONFLICT 33
FT /note="R -> P (in Ref. 3; CAA64689)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="I -> K (in Ref. 3; CAA64689)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="T -> S (in Ref. 3; CAA64689)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="P -> A (in Ref. 3; CAA64689)"
FT /evidence="ECO:0000305"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 128..146
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 304..310
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:1DMR"
FT TURN 322..326
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 343..355
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1DMR"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 373..386
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:1DMR"
FT TURN 403..406
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:4DMR"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 441..443
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 444..449
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 460..463
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 484..490
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 491..493
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 495..503
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 506..509
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 512..517
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 525..529
FT /evidence="ECO:0007829|PDB:1DMR"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 536..540
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 553..563
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 567..571
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 576..593
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 601..607
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 609..611
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 624..628
FT /evidence="ECO:0007829|PDB:1DMR"
FT TURN 630..632
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 640..645
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 647..652
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 679..682
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 687..690
FT /evidence="ECO:0007829|PDB:1DMR"
FT TURN 694..696
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 698..702
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 710..713
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 715..720
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 737..744
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 773..775
FT /evidence="ECO:0007829|PDB:1DMR"
FT HELIX 778..780
FT /evidence="ECO:0007829|PDB:1DMR"
FT TURN 789..791
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 800..805
FT /evidence="ECO:0007829|PDB:1DMR"
FT STRAND 815..817
FT /evidence="ECO:0007829|PDB:1E60"
FT HELIX 820..822
FT /evidence="ECO:0007829|PDB:1DMR"
SQ SEQUENCE 823 AA; 89561 MW; 0E5E901CF2D69273 CRC64;
MTKFSGNELR AELYRRAFLS YSVAPGALGM FGRSLLAKGA RAEALANGTV MSGSHWGVFT
ATVENGRATA FTPWEKDPHP TPMLEGVLDS IYSPTRIKYP MVRREFLEKG VNADRSTRGN
GDFVRVSWDQ ALDLVAAEVK RVEETYGPQG VFGGSYGWKS PGRLHNCTTL LRRMLTLAGG
YVNGAGDYST GAAQVIMPHV VGTLEVYEQQ TAWPVLAENT EVMVFWAADP IKTSQIGWVI
PEHGAYPGLE ALKAKGTKVI VIDPVRTKTV EFFGADHVTP KPQTDVAIML GMAHTLVAED
LYDKDFIANY TSGFDKFLPY LMGETDSTPK TAEWASDISG VPAETIKELA RLFISKRTML
AAGWSMQRMH HGEQAHWMLV TLASMLGQIG LPGGGFGLSY HYSGGGTPST SGPALSGITD
GGAATKGPEW LAASGASVIP VARVVDMLEN PGAEFDFNGT RSKFPDVKMA YWVGGNPFVH
HQDRNRMVKA WEKLETFIVH DFQWTPTARH ADIVLPATTS YERNDIETIG DYSNTGILAM
KKIVEPLYEA RSDYDIFAAV AERLGKGKEF TEGKDEMGWI KSFYDDAAKQ GKAGGVEMPA
FDAFWAEGIV EFPVTDGADF VRYASFREDP LLNPLGTPTG LIEIYSKNIE KMGYDDCPAH
PTWMEPLERL DGPGAKYPLH IAASHPFNRL HSQLNGTVLR EGYAVQGHEP CLMHPDDAAA
RGIADGDVVR VHNDRGQILT GVKVTDAVMK GVIQIYEGGW YDPSDVTEPG TLDKYGDVNV
LSADIGTSKL AQGNCGQTVL AEVEKYTGPA VTLTGFVAPK AAE
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