ID DMSA_ECOLI Reviewed; 814 AA.
AC P18775;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 200.
DE RecName: Full=Dimethyl sulfoxide reductase DmsA;
DE Short=DMSO reductase;
DE Short=DMSOR;
DE Short=Me2SO reductase;
DE EC=1.8.5.3;
DE Flags: Precursor;
GN Name=dmsA; OrderedLocusNames=b0894, JW5118;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 46-51, AND FUNCTION
RP AS A DIMETHYLSULPHOXIDE REDUCTASE.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=3062312; DOI=10.1111/j.1365-2958.1988.tb00090.x;
RA Bilous P.T., Cole S.T., Anderson W.F., Weiner J.H.;
RT "Nucleotide sequence of the dmsABC operon encoding the anaerobic
RT dimethylsulphoxide reductase of Escherichia coli.";
RL Mol. Microbiol. 2:785-795(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP SUBUNIT, AND COFACTOR.
RX PubMed=3280546; DOI=10.1128/jb.170.4.1505-1510.1988;
RA Weiner J.H., MacIsaac D.P., Bishop R.E., Bilous P.T.;
RT "Purification and properties of Escherichia coli dimethyl sulfoxide
RT reductase, an iron-sulfur molybdoenzyme with broad substrate specificity.";
RL J. Bacteriol. 170:1505-1510(1988).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=2170332; DOI=10.1128/jb.172.10.5938-5948.1990;
RA Sambasivarao D., Scraba D.G., Trieber C., Weiner J.H.;
RT "Organization of dimethyl sulfoxide reductase in the plasma membrane of
RT Escherichia coli.";
RL J. Bacteriol. 172:5938-5948(1990).
RN [7]
RP MUTAGENESIS OF LYS-57; CYS-67; CYS-71; CYS-104 AND ARG-106.
RX PubMed=8125918; DOI=10.1016/s0021-9258(17)37253-8;
RA Trieber C.A., Rothery R.A., Weiner J.H.;
RT "Multiple pathways of electron transfer in dimethyl sulfoxide reductase of
RT Escherichia coli.";
RL J. Biol. Chem. 269:7103-7109(1994).
RN [8]
RP COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=7721698; DOI=10.1128/jb.177.8.2057-2063.1995;
RA Rothery R.A., Grant J.L., Johnson J.L., Rajagopalan K.V., Weiner J.H.;
RT "Association of molybdopterin guanine dinucleotide with Escherichia coli
RT dimethyl sulfoxide reductase: effect of tungstate and a mob mutation.";
RL J. Bacteriol. 177:2057-2063(1995).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=8969520; DOI=10.1099/13500872-142-11-3231;
RA Simala-Grant J.L., Weiner J.H.;
RT "Kinetic analysis and substrate specificity of Escherichia coli dimethyl
RT sulfoxide reductase.";
RL Microbiology 142:3231-3239(1996).
RN [10]
RP MUTAGENESIS OF CYS-67 AND ARG-106, AND COFACTOR.
RX PubMed=10224050; DOI=10.1074/jbc.274.19.13002;
RA Rothery R.A., Trieber C.A., Weiner J.H.;
RT "Interactions between the molybdenum cofactor and iron-sulfur clusters of
RT Escherichia coli dimethylsulfoxide reductase.";
RL J. Biol. Chem. 274:13002-13009(1999).
RN [11]
RP EXPORT VIA THE TAT-SYSTEM, AND MUTAGENESIS OF ARG-17.
RX PubMed=10801884; DOI=10.1074/jbc.m909289199;
RA Sambasivarao D., Turner R.J., Simala-Grant J.L., Shaw G., Hu J.,
RA Weiner J.H.;
RT "Multiple roles for the twin arginine leader sequence of dimethyl sulfoxide
RT reductase of Escherichia coli.";
RL J. Biol. Chem. 275:22526-22531(2000).
RN [12]
RP EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [13]
RP INTERACTION OF SIGNAL PEPTIDE WITH DMSD; TATB AND TATC, AND MUTAGENESIS OF
RP 17-ARG-ARG-18.
RX PubMed=20169075; DOI=10.1371/journal.pone.0009225;
RA Kostecki J.S., Li H., Turner R.J., DeLisa M.P.;
RT "Visualizing interactions along the Escherichia coli twin-arginine
RT translocation pathway using protein fragment complementation.";
RL PLoS ONE 5:E9225-E9225(2010).
CC -!- FUNCTION: Catalyzes the reduction of dimethyl sulfoxide (DMSO) to
CC dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase
CC under anaerobic conditions, with DMSO being the terminal electron
CC acceptor. Terminal reductase during anaerobic growth on various
CC sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically
CC on DMSO as respiratory oxidant. {ECO:0000269|PubMed:3062312}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Evidence={ECO:0000269|PubMed:10224050, ECO:0000269|PubMed:3280546,
CC ECO:0000269|PubMed:7721698};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000269|PubMed:10224050,
CC ECO:0000269|PubMed:3280546, ECO:0000269|PubMed:7721698};
CC -!- ACTIVITY REGULATION: Inhibited by dithionite, sodium hydrogensulfite
CC and tungstate. {ECO:0000269|PubMed:7721698,
CC ECO:0000269|PubMed:8969520}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.043 mM for 2-chloropyridine N-oxide (at pH 5 and at 30 degrees
CC Celsius) {ECO:0000269|PubMed:8969520};
CC KM=0.045 mM for 3-amidopyridine N-oxide (at pH 5 and at 30 degrees
CC Celsius) {ECO:0000269|PubMed:8969520};
CC KM=0.06 mM for tertramethylene sulfoxide (at pH 5 and at 30 degrees
CC Celsius) {ECO:0000269|PubMed:8969520};
CC KM=0.09 mM for methionine sulfoxide (at pH 5 and at 30 degrees
CC Celsius) {ECO:0000269|PubMed:8969520};
CC KM=0.246 mM for 4-phenylpyridine N-oxide (at pH 5 and at 30 degrees
CC Celsius) {ECO:0000269|PubMed:8969520};
CC KM=0.830 mM for dimethyldodecylamin N-oxide (at pH 5 and at 30
CC degrees Celsius) {ECO:0000269|PubMed:8969520};
CC KM=0.18 mM for DMSO (at pH 6.8 and at 23 degrees Celsius)
CC {ECO:0000269|PubMed:3280546};
CC KM=0.47 mM for L-methionine sulfoxide (at pH 6.8 and at 23 degrees
CC Celsius) {ECO:0000269|PubMed:3280546};
CC KM=0.5 mM for nicotinamide N-oxide (at pH 6.8 and at 23 degrees
CC Celsius) {ECO:0000269|PubMed:3280546};
CC KM=0.6 mM for TMAO (at pH 6.8 and at 23 degrees Celsius)
CC {ECO:0000269|PubMed:3280546};
CC KM=1.0 mM for 4-picoline N-oxide (at pH 6.8 and at 23 degrees
CC Celsius) {ECO:0000269|PubMed:3280546};
CC KM=20.2 mM for TMAO (at pH 5 and at 30 degrees Celsius)
CC {ECO:0000269|PubMed:8969520};
CC -!- SUBUNIT: Heterotrimeric enzyme composed of a catalytic heterodimer
CC (DmsAB) and a membrane anchor protein (DmsC).
CC {ECO:0000269|PubMed:3280546}.
CC -!- INTERACTION:
CC P18775; P18776: dmsB; NbExp=2; IntAct=EBI-4411104, EBI-1120825;
CC P18775; P69853: dmsD; NbExp=8; IntAct=EBI-4411104, EBI-4406374;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2170332,
CC ECO:0000269|PubMed:3280546}; Peripheral membrane protein
CC {ECO:0000269|PubMed:2170332, ECO:0000269|PubMed:3280546}; Cytoplasmic
CC side {ECO:0000269|PubMed:2170332, ECO:0000269|PubMed:3280546}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has been experimentally proven. Can also be exported by the
CC Sec system.
CC -!- MISCELLANEOUS: The Tat signal sequence is essential for the expression
CC of dmsA, the stability of the DmsAB dimer and membrane targeting.
CC Despite the presence of a signal sequence, DmsA is not exported to the
CC periplasm.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83843.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; J03412; AAA83843.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73980.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35626.2; -; Genomic_DNA.
DR PIR; S03785; S03785.
DR RefSeq; NP_415414.4; NC_000913.3.
DR RefSeq; WP_000850303.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P18775; -.
DR SMR; P18775; -.
DR BioGRID; 4261945; 69.
DR BioGRID; 849882; 3.
DR ComplexPortal; CPX-320; DmaABC DMSO reductase complex.
DR DIP; DIP-9452N; -.
DR IntAct; P18775; 8.
DR MINT; P18775; -.
DR STRING; 511145.b0894; -.
DR TCDB; 5.A.3.3.2; the prokaryotic molybdopterin-containing oxidoreductase (pmo) family.
DR jPOST; P18775; -.
DR PaxDb; 511145-b0894; -.
DR EnsemblBacteria; AAC73980; AAC73980; b0894.
DR GeneID; 75170969; -.
DR GeneID; 945508; -.
DR KEGG; ecj:JW5118; -.
DR KEGG; eco:b0894; -.
DR PATRIC; fig|1411691.4.peg.1383; -.
DR EchoBASE; EB0228; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR InParanoid; P18775; -.
DR OMA; IPMFLWT; -.
DR OrthoDB; 9815647at2; -.
DR PhylomeDB; P18775; -.
DR BioCyc; EcoCyc:DMSA-MONOMER; -.
DR BioCyc; MetaCyc:DMSA-MONOMER; -.
DR BRENDA; 1.8.5.3; 2026.
DR PRO; PR:P18775; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009390; C:dimethyl sulfoxide reductase complex; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IMP:EcoCyc.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IMP:EcoCyc.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IEP:EcoCyc.
DR GO; GO:0018907; P:dimethyl sulfoxide metabolic process; IDA:ComplexPortal.
DR CDD; cd02794; MopB_CT_DmsA-EC; 1.
DR CDD; cd02770; MopB_DmsA-EC; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 2.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR011888; Anaer_DMSO_reductase.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE 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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell membrane; Direct protein sequencing; Iron; Iron-sulfur;
KW Membrane; Metal-binding; Molybdenum; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..45
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:3062312"
FT CHAIN 46..814
FT /note="Dimethyl sulfoxide reductase DmsA"
FT /id="PRO_0000019143"
FT DOMAIN 56..118
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 172..176
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 205
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 /evidence="ECO:0000250"
FT BINDING 244..245
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 270..271
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 291..293
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 386..387
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 512..513
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 701
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 707..709
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 788
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT BINDING 804..805
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000250"
FT MUTAGEN 17
FT /note="R->S: Not targeted to the membrane, does not support
FT anaerobic growth."
FT /evidence="ECO:0000269|PubMed:10801884"
FT MUTAGEN 57
FT /note="K->D: No alteration of the growth, expression, or
FT catalytic activities."
FT /evidence="ECO:0000269|PubMed:8125918"
FT MUTAGEN 67
FT /note="C->S: Electron transfer from the 4Fe-4S clusters of
FT DmsB to the Mo-bisMGD of DmsA is blocked. Little effect on
FT the coordination sphere of the molybdenum and only minor
FT effects on its redox chemistry."
FT /evidence="ECO:0000269|PubMed:10224050,
FT ECO:0000269|PubMed:8125918"
FT MUTAGEN 71
FT /note="C->S: Cannot support growth."
FT /evidence="ECO:0000269|PubMed:8125918"
FT MUTAGEN 104
FT /note="C->S: No alteration of the growth, expression, or
FT catalytic activities."
FT /evidence="ECO:0000269|PubMed:8125918"
FT MUTAGEN 106
FT /note="R->S: Electron transfer from the 4Fe-4S clusters of
FT DmsB to the Mo-bisMGD of DmsA is blocked. Little effect on
FT the coordination sphere of the molybdenum and only minor
FT effects on its redox chemistry."
FT /evidence="ECO:0000269|PubMed:10224050,
FT ECO:0000269|PubMed:8125918"
SQ SEQUENCE 814 AA; 90399 MW; B97C830ABAC7C32C CRC64;
MKTKIPDAVL AAEVSRRGLV KTTAIGGLAM ASSALTLPFS RIAHAVDSAI PTKSDEKVIW
SACTVNCGSR CPLRMHVVDG EIKYVETDNT GDDNYDGLHQ VRACLRGRSM RRRVYNPDRL
KYPMKRVGAR GEGKFERISW EEAYDIIATN MQRLIKEYGN ESIYLNYGTG TLGGTMTRSW
PPGNTLVARL MNCCGGYLNH YGDYSSAQIA EGLNYTYGGW ADGNSPSDIE NSKLVVLFGN
NPGETRMSGG GVTYYLEQAR QKSNARMIII DPRYTDTGAG REDEWIPIRP GTDAALVNGL
AYVMITENLV DQAFLDKYCV GYDEKTLPAS APKNGHYKAY ILGEGPDGVA KTPEWASQIT
GVPADKIIKL AREIGSTKPA FISQGWGPQR HANGEIATRA ISMLAILTGN VGINGGNSGA
REGSYSLPFV RMPTLENPIQ TSISMFMWTD AIERGPEMTA LRDGVRGKDK LDVPIKMIWN
YAGNCLINQH SEINRTHEIL QDDKKCELIV VIDCHMTSSA KYADILLPDC TASEQMDFAL
DASCGNMSYV IFNDQVIKPR FECKTIYEMT SELAKRLGVE QQFTEGRTQE EWMRHLYAQS
REAIPELPTF EEFRKQGIFK KRDPQGHHVA YKAFREDPQA NPLTTPSGKI EIYSQALADI
AATWELPEGD VIDPLPIYTP GFESYQDPLN KQYPLQLTGF HYKSRVHSTY GNVDVLKAAC
RQEMWINPLD AQKRGIHNGD KVRIFNDRGE VHIEAKVTPR MMPGVVALGE GAWYDPDAKR
VDKGGCINVL TTQRPSPLAK GNPSHTNLVQ VEKV
//
