FDHF_ECOLI
ID FDHF_ECOLI Reviewed; 715 AA.
AC P07658; P78137; Q2M6M5;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Formate dehydrogenase H;
DE EC=1.17.98.4 {ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855, ECO:0000269|PubMed:9521673};
DE AltName: Full=Formate dehydrogenase-H subunit alpha;
DE Short=FDH-H;
DE AltName: Full=Formate-hydrogen-lyase-linked, selenocysteine-containing polypeptide;
GN Name=fdhF; OrderedLocusNames=b4079, JW4040;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=2941757; DOI=10.1073/pnas.83.13.4650;
RA Zinoni F., Birkmann A., Stadtman T.C., Boeck A.;
RT "Nucleotide sequence and expression of the selenocysteine-containing
RT polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from
RT Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4650-4654(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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 PROTEIN SEQUENCE OF 1-12, AND CHARACTERIZATION.
RX PubMed=2211698; DOI=10.1016/s0021-9258(17)44740-5;
RA Axley M.J., Grahame D.A., Stadtman T.C.;
RT "Escherichia coli formate-hydrogen lyase. Purification and properties of
RT the selenium-dependent formate dehydrogenase component.";
RL J. Biol. Chem. 265:18213-18218(1990).
RN [6]
RP ACTIVITY REGULATION, AND CRYSTALLIZATION.
RX PubMed=8626495; DOI=10.1074/jbc.271.14.8095;
RA Gladyshev V.N., Boyington J.C., Khangulov S.V., Grahame D.A.,
RA Stadtman T.C., Sun P.D.;
RT "Characterization of crystalline formate dehydrogenase H from Escherichia
RT coli. Stabilization, EPR spectroscopy, and preliminary crystallographic
RT analysis.";
RL J. Biol. Chem. 271:8095-8100(1996).
RN [7]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=9521673; DOI=10.1021/bi972177k;
RA Khangulov S.V., Gladyshev V.N., Dismukes G.C., Stadtman T.C.;
RT "Selenium-containing formate dehydrogenase H from Escherichia coli: a
RT molybdopterin enzyme that catalyzes formate oxidation without oxygen
RT transfer.";
RL Biochemistry 37:3518-3528(1998).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR
RP (4FE-4S); MOLYBDENUM ION AND MOLYBDOPTERIN, SELENOCYSTEINE AT SEC-140,
RP COFACTOR, AND CATALYTIC ACTIVITY.
RX PubMed=9036855; DOI=10.1126/science.275.5304.1305;
RA Boyington J.C., Gladyshev V.N., Khangulov S.V., Stadtman T.C., Sun P.D.;
RT "Crystal structure of formate dehydrogenase H: catalysis involving Mo,
RT molybdopterin, selenocysteine, and an Fe4S4 cluster.";
RL Science 275:1305-1308(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S)
RP AND MOLYBDOPTERIN, AND CATALYTIC ACTIVITY.
RX PubMed=16830149; DOI=10.1007/s00775-006-0129-2;
RA Raaijmakers H.C., Romao M.J.;
RT "Formate-reduced E. coli formate dehydrogenase H: The reinterpretation of
RT the crystal structure suggests a new reaction mechanism.";
RL J. Biol. Inorg. Chem. 11:849-854(2006).
CC -!- FUNCTION: Decomposes formic acid to hydrogen and carbon dioxide under
CC anaerobic conditions in the absence of exogenous electron acceptors.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + formate + H(+) = AH2 + CO2; Xref=Rhea:RHEA:27290,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17499; EC=1.17.98.4;
CC Evidence={ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855,
CC ECO:0000269|PubMed:9521673};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539;
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit.;
CC -!- ACTIVITY REGULATION: Inhibited by aerobic conditions.
CC {ECO:0000269|PubMed:8626495, ECO:0000269|PubMed:9521673}.
CC -!- SUBUNIT: Consists of two separable enzymatic activities: a formate
CC dehydrogenase component (FDH-H) and hydrogenase-3.
CC {ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855}.
CC -!- INTERACTION:
CC P07658; P16433: hycG; NbExp=3; IntAct=EBI-1121603, EBI-541977;
CC -!- INDUCTION: By formate. Repressed by oxygen, nitrate, nitrite, and other
CC electron acceptors.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; M13563; AAA23754.2; -; Genomic_DNA.
DR EMBL; U00006; AAC43173.2; -; Genomic_DNA.
DR EMBL; U00096; AAD13462.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78081.1; -; Genomic_DNA.
DR PIR; A24145; DEECFS.
DR RefSeq; NP_418503.1; NC_000913.3.
DR RefSeq; WP_001300547.1; NZ_STEB01000014.1.
DR PDB; 1AA6; X-ray; 2.30 A; A=1-715.
DR PDB; 1FDI; X-ray; 2.90 A; A=1-715.
DR PDB; 1FDO; X-ray; 2.80 A; A=1-715.
DR PDB; 2IV2; X-ray; 2.27 A; X=1-715.
DR PDBsum; 1AA6; -.
DR PDBsum; 1FDI; -.
DR PDBsum; 1FDO; -.
DR PDBsum; 2IV2; -.
DR SMR; P07658; -.
DR BioGRID; 4262950; 28.
DR BioGRID; 852878; 1.
DR ComplexPortal; CPX-317; Formate hydrogenlyase-H/Hydrogenase-3 complex.
DR ComplexPortal; CPX-6028; Formate hydrogenlyase-H/Hydrogenase-4 complex.
DR DIP; DIP-9572N; -.
DR IntAct; P07658; 14.
DR STRING; 511145.b4079; -.
DR DrugBank; DB02345; Selenocysteine.
DR TCDB; 3.D.1.9.2; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P07658; -.
DR PaxDb; P07658; -.
DR PRIDE; P07658; -.
DR GeneID; 66672005; -.
DR GeneID; 948584; -.
DR KEGG; ecj:JW4040; -.
DR KEGG; eco:b4079; -.
DR PATRIC; fig|511145.12.peg.4203; -.
DR EchoBASE; EB0281; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_6; -.
DR InParanoid; P07658; -.
DR OMA; NVGTDIP; -.
DR PhylomeDB; P07658; -.
DR BioCyc; EcoCyc:FORMATEDEHYDROGH-MON; -.
DR BioCyc; MetaCyc:FORMATEDEHYDROGH-MON; -.
DR BRENDA; 1.17.1.9; 2026.
DR BRENDA; 1.17.98.4; 2026.
DR EvolutionaryTrace; P07658; -.
DR PRO; PR:P07658; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009326; C:formate dehydrogenase complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:EcoCyc.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IDA:EcoCyc.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IDA:ComplexPortal.
DR GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
DR GO; GO:0015944; P:formate oxidation; IDA:ComplexPortal.
DR GO; GO:0006007; P:glucose catabolic process; IDA:ComplexPortal.
DR GO; GO:0019628; P:urate catabolic process; IMP:EcoCyc.
DR CDD; cd02790; MopB_CT_Formate-Dh_H; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
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 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; TIGR01591; Fdh-alpha; 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.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Molybdenum; NAD; Oxidoreductase; Reference proteome;
KW Selenocysteine.
FT CHAIN 1..715
FT /note="Formate dehydrogenase H"
FT /id="PRO_0000063221"
FT DOMAIN 1..56
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT ACT_SITE 44
FT /note="Electron donor/acceptor"
FT ACT_SITE 140
FT /note="Proton donor/acceptor"
FT BINDING 8
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004,
FT ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855"
FT BINDING 10
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004,
FT ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855"
FT BINDING 11
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004,
FT ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855"
FT BINDING 15
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004,
FT ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004,
FT ECO:0000269|PubMed:16830149, ECO:0000269|PubMed:9036855"
FT BINDING 44
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT BINDING 110..112
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 140
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 173..180
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 201..204
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 221..223
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 297
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT BINDING 301
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT BINDING 335
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT BINDING 402..410
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 428..429
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 445
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT BINDING 478
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT BINDING 579..581
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 581..587
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 588
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT BINDING 654
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT BINDING 655
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT BINDING 661..662
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT BINDING 678
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT BINDING 679
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /evidence="ECO:0000269|PubMed:16830149,
FT ECO:0000269|PubMed:9036855"
FT SITE 141
FT /note="Important for catalytic activity"
FT SITE 333
FT /note="Important for catalytic activity"
FT NON_STD 140
FT /note="Selenocysteine"
FT /evidence="ECO:0000269|PubMed:9036855"
FT CONFLICT 19
FT /note="L -> V (in Ref. 1; AAA23754)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:2IV2"
FT TURN 35..39
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1AA6"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:1AA6"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 252..260
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 305..318
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 360..369
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 383..385
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 386..391
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 412..421
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 422..431
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 440..445
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:1AA6"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 478..488
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 498..508
FT /evidence="ECO:0007829|PDB:2IV2"
FT TURN 510..514
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 517..520
FT /evidence="ECO:0007829|PDB:2IV2"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:1FDI"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 575..579
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:1FDI"
FT HELIX 592..594
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 596..599
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 607..611
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 612..618
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 634..645
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 649..652
FT /evidence="ECO:0007829|PDB:2IV2"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:1FDI"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:1FDO"
FT TURN 671..673
FT /evidence="ECO:0007829|PDB:1FDO"
FT STRAND 681..687
FT /evidence="ECO:0007829|PDB:2IV2"
FT HELIX 691..713
FT /evidence="ECO:0007829|PDB:2IV2"
SQ SEQUENCE 715 AA; 79374 MW; C7C86F6F704A142D CRC64;
MKKVVTVCPY CASGCKINLV VDNGKIVRAE AAQGKTNQGT LCLKGYYGWD FINDTQILTP
RLKTPMIRRQ RGGKLEPVSW DEALNYVAER LSAIKEKYGP DAIQTTGSSR GTGNETNYVM
QKFARAVIGT NNVDCCARVU HGPSVAGLHQ SVGNGAMSNA INEIDNTDLV FVFGYNPADS
HPIVANHVIN AKRNGAKIIV CDPRKIETAR IADMHIALKN GSNIALLNAM GHVIIEENLY
DKAFVASRTE GFEEYRKIVE GYTPESVEDI TGVSASEIRQ AARMYAQAKS AAILWGMGVT
QFYQGVETVR SLTSLAMLTG NLGKPHAGVN PVRGQNNVQG ACDMGALPDT YPGYQYVKDP
ANREKFAKAW GVESLPAHTG YRISELPHRA AHGEVRAAYI MGEDPLQTDA ELSAVRKAFE
DLELVIVQDI FMTKTASAAD VILPSTSWGE HEGVFTAADR GFQRFFKAVE PKWDLKTDWQ
IISEIATRMG YPMHYNNTQE IWDELRHLCP DFYGATYEKM GELGFIQWPC RDTSDADQGT
SYLFKEKFDT PNGLAQFFTC DWVAPIDKLT DEYPMVLSTV REVGHYSCRS MTGNCAALAA
LADEPGYAQI NTEDAKRLGI EDEALVWVHS RKGKIITRAQ VSDRPNKGAI YMTYQWWIGA
CNELVTENLS PITKTPEYKY CAVRVEPIAD QRAAEQYVID EYNKLKTRLR EAALA
