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   27-MAR-2024, entry version 220.
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; Pseudomonadota; 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}.
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; M13563; AAA23754.3; -; 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   PDB; 7Z0T; EM; 3.40 A; A=1-715.
DR   PDBsum; 1AA6; -.
DR   PDBsum; 1FDI; -.
DR   PDBsum; 1FDO; -.
DR   PDBsum; 2IV2; -.
DR   PDBsum; 7Z0T; -.
DR   EMDB; EMD-14430; -.
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; 511145-b4079; -.
DR   GeneID; 75203235; -.
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; PEYKHCA; -.
DR   OrthoDB; 9810782at2; -.
DR   PhylomeDB; P07658; -.
DR   BioCyc; EcoCyc:FORMATEDEHYDROGH-MONOMER; -.
DR   BioCyc; MetaCyc:FORMATEDEHYDROGH-MONOMER; -.
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; NAS: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   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   Gene3D; 1.20.5.460; Single helix bin; 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   NCBIfam; TIGR01591; Fdh-alpha; 1.
DR   PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 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   PIRSF; PIRSF000144; CbbBc; 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.
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
//