ID   ALGD_PSEAE              Reviewed;         436 AA.
AC   P11759; Q9HY71;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=GDP-mannose 6-dehydrogenase {ECO:0000303|PubMed:3108855};
DE            Short=GMD {ECO:0000303|PubMed:3108855};
DE            EC=1.1.1.132 {ECO:0000269|PubMed:2470755};
DE   AltName: Full=Guanosine diphospho-D-mannose dehydrogenase {ECO:0000303|PubMed:1370473};
GN   Name=algD {ECO:0000303|PubMed:3108855}; OrderedLocusNames=PA3540;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND INDUCTION.
RC   STRAIN=8830;
RX   PubMed=3108855; DOI=10.1093/nar/15.11.4567;
RA   Deretic V., Gill J.F., Chakrabarty A.M.;
RT   "Pseudomonas aeruginosa infection in cystic fibrosis: nucleotide sequence
RT   and transcriptional regulation of the algD gene.";
RL   Nucleic Acids Res. 15:4567-4581(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC   STRAIN=8830;
RX   PubMed=2470755; DOI=10.1016/s0021-9258(18)60542-3;
RA   Roychoudhury S., May T.B., Gill J.F., Singh S.K., Feingold D.S.,
RA   Chakrabarty A.M.;
RT   "Purification and characterization of guanosine diphospho-D-mannose
RT   dehydrogenase. A key enzyme in the biosynthesis of alginate by Pseudomonas
RT   aeruginosa.";
RL   J. Biol. Chem. 264:9380-9385(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-11; 280-289 AND 297-306, CATALYTIC ACTIVITY, AND
RP   DOMAIN.
RC   STRAIN=8830;
RX   PubMed=1370473; DOI=10.1016/s0021-9258(18)48384-6;
RA   Roychoudhury S., Chakrabarty K., Ho Y.-K., Chakrabarty A.M.;
RT   "Characterization of guanosine diphospho-D-mannose dehydrogenase from
RT   Pseudomonas aeruginosa. Structural analysis by limited proteolysis.";
RL   J. Biol. Chem. 267:990-996(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 425-435.
RC   STRAIN=8830;
RX   PubMed=8294014; DOI=10.1016/0378-1119(93)90477-k;
RA   Maharaj R., May T.B., Wang S.-K., Chakrabarty A.M.;
RT   "Sequence of the alg8 and alg44 genes involved in the synthesis of alginate
RT   by Pseudomonas aeruginosa.";
RL   Gene 136:267-269(1993).
RN   [6]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=12135385; DOI=10.1021/bi025862m;
RA   Naught L.E., Gilbert S., Imhoff R., Snook C., Beamer L., Tipton P.;
RT   "Allosterism and cooperativity in Pseudomonas aeruginosa GDP-mannose
RT   dehydrogenase.";
RL   Biochemistry 41:9637-9645(2002).
RN   [7] {ECO:0007744|PDB:1MFZ, ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8}
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEXES WITH NAD AND
RP   GDP-ALPHA-D-MANNURONATE, FUNCTION, ACTIVE SITE, SUBUNIT, AND PATHWAY.
RX   PubMed=12705829; DOI=10.1021/bi027328k;
RA   Snook C.F., Tipton P.A., Beamer L.J.;
RT   "Crystal structure of GDP-mannose dehydrogenase: a key enzyme of alginate
RT   biosynthesis in P. aeruginosa.";
RL   Biochemistry 42:4658-4668(2003).
CC   -!- FUNCTION: Catalyzes the oxidation of guanosine diphospho-D-mannose
CC       (GDP-D-mannose) to GDP-D-mannuronic acid, a precursor for alginate
CC       polymerization. The alginate layer causes a mucoid phenotype and
CC       provides a protective barrier against host immune defenses and
CC       antibiotics (Probable). Other sugars are not used as substrates
CC       (PubMed:2470755). {ECO:0000269|PubMed:2470755,
CC       ECO:0000305|PubMed:12705829, ECO:0000305|PubMed:2470755,
CC       ECO:0000305|PubMed:3108855}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-alpha-D-mannose + H2O + 2 NAD(+) = GDP-alpha-D-mannuronate
CC         + 3 H(+) + 2 NADH; Xref=Rhea:RHEA:21728, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:84886; EC=1.1.1.132;
CC         Evidence={ECO:0000269|PubMed:12135385, ECO:0000269|PubMed:1370473,
CC         ECO:0000269|PubMed:2470755};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21729;
CC         Evidence={ECO:0000269|PubMed:12135385, ECO:0000269|PubMed:1370473,
CC         ECO:0000269|PubMed:2470755};
CC   -!- ACTIVITY REGULATION: Inhibited by GMP, ATP, GDP-D-glucose and maltose
CC       (PubMed:2470755). Inhibited by GMP and deamidoNAD (PubMed:12135385).
CC       {ECO:0000269|PubMed:12135385, ECO:0000269|PubMed:2470755}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=14.9 uM for GDP-D-mannose {ECO:0000269|PubMed:2470755};
CC         KM=4.1 uM for GDP-D-mannose {ECO:0000269|PubMed:12135385};
CC         KM=185 uM for NAD(+) {ECO:0000269|PubMed:2470755};
CC         KM=92 uM for NAD(+) {ECO:0000269|PubMed:12135385};
CC         Vmax=581.4 nmol/min/mg enzyme {ECO:0000269|PubMed:2470755};
CC       pH dependence:
CC         Optimum pH is 7.7. {ECO:0000269|PubMed:2470755};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius. Stable at 57.5 degrees
CC         Celsius, pH 5.0 for 10 minutes, used to purify protein.
CC         {ECO:0000269|PubMed:2470755};
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC       {ECO:0000305|PubMed:12705829, ECO:0000305|PubMed:3108855}.
CC   -!- SUBUNIT: Forms a domain-swapped dimer with each peptide contributing to
CC       each active site. The dimers assemble further (PubMed:12705829). X-ray
CC       structures indicate this enzyme exists as a homotetramer
CC       PubMed:12705829, but kinetic and physical results obtained in
CC       PubMed:2470755 and PubMed:12135385 indicate that it is probably a
CC       homohexamer (Probable). {ECO:0000269|PubMed:12705829,
CC       ECO:0000305|PubMed:12135385, ECO:0000305|PubMed:12705829,
CC       ECO:0000305|PubMed:2470755}.
CC   -!- INDUCTION: Highly expressed in mucoid but not non-mucoid cells,
CC       probably activated by algR. {ECO:0000269|PubMed:3108855}.
CC   -!- DOMAIN: The N-terminus (about 270 residues) binds NAD(+) and GDP-alpha-
CC       D-mannose and is joined to C-terminal domain by an exposed linker.
CC       {ECO:0000269|PubMed:1370473}.
CC   -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase
CC       family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Slime with a design - Issue
CC       37 of August 2003;
CC       URL="https://web.expasy.org/spotlight/back_issues/037";
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; Y00337; CAA68425.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06928.1; -; Genomic_DNA.
DR   EMBL; L22611; AAC36874.1; -; Genomic_DNA.
DR   PIR; H83203; H83203.
DR   PIR; S07391; DEPSGD.
DR   RefSeq; NP_252230.1; NC_002516.2.
DR   RefSeq; WP_003110461.1; NZ_QZGE01000001.1.
DR   PDB; 1MFZ; X-ray; 2.80 A; A/B/C/D=1-436.
DR   PDB; 1MUU; X-ray; 2.02 A; A/B/C/D=1-436.
DR   PDB; 1MV8; X-ray; 1.55 A; A/B/C/D=1-436.
DR   PDBsum; 1MFZ; -.
DR   PDBsum; 1MUU; -.
DR   PDBsum; 1MV8; -.
DR   AlphaFoldDB; P11759; -.
DR   SMR; P11759; -.
DR   STRING; 208964.PA3540; -.
DR   DrugBank; DB04023; GDP-alpha-D-mannuronic acid.
DR   PaxDb; 208964-PA3540; -.
DR   GeneID; 879004; -.
DR   KEGG; pae:PA3540; -.
DR   PATRIC; fig|208964.12.peg.3704; -.
DR   PseudoCAP; PA3540; -.
DR   HOGENOM; CLU_023810_1_1_6; -.
DR   InParanoid; P11759; -.
DR   OrthoDB; 9803238at2; -.
DR   PhylomeDB; P11759; -.
DR   BioCyc; MetaCyc:MONOMER-14396; -.
DR   BioCyc; PAER208964:G1FZ6-3608-MONOMER; -.
DR   BRENDA; 1.1.1.132; 5087.
DR   UniPathway; UPA00286; -.
DR   EvolutionaryTrace; P11759; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0047919; F:GDP-mannose 6-dehydrogenase activity; IDA:PseudoCAP.
DR   GO; GO:0051287; F:NAD binding; IDA:PseudoCAP.
DR   GO; GO:0042121; P:alginic acid biosynthetic process; IDA:PseudoCAP.
DR   GO; GO:0036460; P:cellular response to cell envelope stress; IDA:PseudoCAP.
DR   GO; GO:0006970; P:response to osmotic stress; IDA:PseudoCAP.
DR   GO; GO:0044010; P:single-species biofilm formation; IDA:PseudoCAP.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR028358; GDPman_DH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR017476; UDP-Glc/GDP-Man.
DR   InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C.
DR   InterPro; IPR036220; UDP-Glc/GDP-Man_DH_C_sf.
DR   InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer.
DR   InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N.
DR   NCBIfam; TIGR03026; NDP-sugDHase; 1.
DR   PANTHER; PTHR43750:SF1; GDP-MANNOSE 6-DEHYDROGENASE; 1.
DR   PANTHER; PTHR43750; UDP-GLUCOSE 6-DEHYDROGENASE TUAD; 1.
DR   Pfam; PF00984; UDPG_MGDP_dh; 1.
DR   Pfam; PF03720; UDPG_MGDP_dh_C; 1.
DR   Pfam; PF03721; UDPG_MGDP_dh_N; 1.
DR   PIRSF; PIRSF500135; GDPman_DH; 1.
DR   PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1.
DR   SMART; SM00984; UDPG_MGDP_dh_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52413; UDP-glucose/GDP-mannose dehydrogenase C-terminal domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alginate biosynthesis; Direct protein sequencing; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..436
FT                   /note="GDP-mannose 6-dehydrogenase"
FT                   /id="PRO_0000074067"
FT   REGION          278..295
FT                   /note="Inter-domain linker"
FT                   /evidence="ECO:0000269|PubMed:1370473"
FT   ACT_SITE        268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:12705829"
FT   BINDING         10
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8"
FT   BINDING         11
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8"
FT   BINDING         30
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8"
FT   BINDING         86
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8"
FT   BINDING         124
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8"
FT   BINDING         161
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         210
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         214
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         217
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         225
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain A"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         256
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain B"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         257
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain B"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         259
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain B"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         262
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain B"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         265
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain B"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain B"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8"
FT   BINDING         324
FT                   /ligand="GDP-alpha-D-mannuronate"
FT                   /ligand_id="ChEBI:CHEBI:84886"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain B"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU"
FT   BINDING         331
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between homodimeric partners"
FT                   /note="in chain B"
FT                   /evidence="ECO:0000269|PubMed:12705829,
FT                   ECO:0007744|PDB:1MUU, ECO:0007744|PDB:1MV8"
FT   VARIANT         349
FT                   /note="L -> F (in strain: 3380)"
FT                   /evidence="ECO:0000305|PubMed:12135385"
FT   STRAND          2..6
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           12..21
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           33..40
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           51..60
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          64..68
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           70..75
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          78..82
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           97..110
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          118..121
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           129..132
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           134..142
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   TURN            147..149
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          150..154
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           164..169
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          174..180
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           181..191
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           203..233
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           238..245
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   TURN            249..253
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          266..268
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           269..282
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           290..292
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           293..308
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          315..319
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          322..324
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           334..344
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          348..352
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           354..359
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          362..364
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           366..371
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           374..377
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           384..390
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          392..396
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           401..403
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   HELIX           404..408
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          415..421
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          424..426
FT                   /evidence="ECO:0007829|PDB:1MV8"
FT   STRAND          429..434
FT                   /evidence="ECO:0007829|PDB:1MV8"
SQ   SEQUENCE   436 AA;  47600 MW;  B6F3DC2B70B04463 CRC64;
     MRISIFGLGY VGAVCAGCLS ARGHEVIGVD VSSTKIDLIN QGKSPIVEPG LEALLQQGRQ
     TGRLSGTTDF KKAVLDSDVS FICVGTPSKK NGDLDLGYIE TVCREIGFAI REKSERHTVV
     VRSTVLPGTV NNVVIPLIED CSGKKAGVDF GVGTNPEFLR ESTAIKDYDF PPMTVIGELD
     KQTGDLLEEI YRELDAPIIR KTVEVAEMIK YTCNVWHAAK VTFANEIGNI AKAVGVDGRE
     VMDVICQDHK LNLSRYYMRP GFAFGGSCLP KDVRALTYRA SQLDVEHPML GSLMRSNSNQ
     VQKAFDLITS HDTRKVGLLG LSFKAGTDDL RESPLVELAE MLIGKGYELR IFDRNVEYAR
     VHGANKEYIE SKIPHVSSLL VSDLDEVVAS SDVLVLGNGD ELFVDLVNKT PSGKKLVDLV
     GFMPHTTTAQ AEGICW
//