6PGD_HUMAN
ID 6PGD_HUMAN Reviewed; 483 AA.
AC P52209; A8K2Y9; B4DQJ8; Q9BWD8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=6-phosphogluconate dehydrogenase, decarboxylating;
DE EC=1.1.1.44;
GN Name=PGD; Synonyms=PGDH;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=8978909; DOI=10.1007/bf00554412;
RA Tsui S.K.W., Chan J.Y., Waye M.M.Y., Fung K.-P., Lee C.-Y.;
RT "Identification of a cDNA encoding 6-phosphogluconate dehydrogenase from a
RT human heart cDNA library.";
RL Biochem. Genet. 34:367-373(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59 AND LYS-309, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH NADP, AND SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Structure of human phosphogluconate dehydrogenase in complex with NADPH at
RT 2.53 A.";
RL Submitted (SEP-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate
CC to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP
CC to NADPH. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-gluconate + NADP(+) = CO2 + D-ribulose 5-phosphate
CC + NADPH; Xref=Rhea:RHEA:10116, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58349, ChEBI:CHEBI:58759; EC=1.1.1.44;
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 3/3.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P52209-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52209-2; Sequence=VSP_055767;
CC -!- SIMILARITY: Belongs to the 6-phosphogluconate dehydrogenase family.
CC {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; U30255; AAA75302.1; -; mRNA.
DR EMBL; AK290404; BAF83093.1; -; mRNA.
DR EMBL; AK298830; BAG60960.1; -; mRNA.
DR EMBL; AL139424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71648.1; -; Genomic_DNA.
DR EMBL; BC000368; AAH00368.1; -; mRNA.
DR CCDS; CCDS113.1; -. [P52209-1]
DR PIR; G01922; G01922.
DR RefSeq; NP_001291380.1; NM_001304451.1.
DR RefSeq; NP_001291381.1; NM_001304452.1. [P52209-2]
DR RefSeq; NP_002622.2; NM_002631.3. [P52209-1]
DR PDB; 2JKV; X-ray; 2.53 A; A/B/C/D/E/F=1-483.
DR PDB; 4GWG; X-ray; 1.39 A; A=2-483.
DR PDB; 4GWK; X-ray; 1.53 A; A=2-483.
DR PDB; 5UQ9; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-483.
DR PDBsum; 2JKV; -.
DR PDBsum; 4GWG; -.
DR PDBsum; 4GWK; -.
DR PDBsum; 5UQ9; -.
DR AlphaFoldDB; P52209; -.
DR SMR; P52209; -.
DR BioGRID; 111247; 141.
DR IntAct; P52209; 33.
DR MINT; P52209; -.
DR STRING; 9606.ENSP00000270776; -.
DR BindingDB; P52209; -.
DR ChEMBL; CHEMBL3404; -.
DR DrugBank; DB02076; 6-phospho-D-gluconic acid.
DR DrugBank; DB00851; Dacarbazine.
DR DrugBank; DB00695; Furosemide.
DR DrugBank; DB00789; Gadopentetic acid.
DR DrugBank; DB00920; Ketotifen.
DR DrugBank; DB00814; Meloxicam.
DR DrugBank; DB00563; Methotrexate.
DR DrugBank; DB03962; Nicotinamide 8-bromo-adenine dinucleotide phosphate.
DR DrugBank; DB00867; Ritodrine.
DR GlyGen; P52209; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P52209; -.
DR MetOSite; P52209; -.
DR PhosphoSitePlus; P52209; -.
DR SwissPalm; P52209; -.
DR BioMuta; PGD; -.
DR DMDM; 20981679; -.
DR CPTAC; CPTAC-560; -.
DR CPTAC; CPTAC-561; -.
DR EPD; P52209; -.
DR jPOST; P52209; -.
DR MassIVE; P52209; -.
DR MaxQB; P52209; -.
DR PaxDb; P52209; -.
DR PeptideAtlas; P52209; -.
DR PRIDE; P52209; -.
DR ProteomicsDB; 4884; -.
DR ProteomicsDB; 56472; -. [P52209-1]
DR TopDownProteomics; P52209-1; -. [P52209-1]
DR Antibodypedia; 27894; 346 antibodies from 33 providers.
DR DNASU; 5226; -.
DR Ensembl; ENST00000270776.13; ENSP00000270776.8; ENSG00000142657.21. [P52209-1]
DR GeneID; 5226; -.
DR KEGG; hsa:5226; -.
DR MANE-Select; ENST00000270776.13; ENSP00000270776.8; NM_002631.4; NP_002622.2.
DR UCSC; uc001arc.4; human. [P52209-1]
DR CTD; 5226; -.
DR DisGeNET; 5226; -.
DR GeneCards; PGD; -.
DR HGNC; HGNC:8891; PGD.
DR HPA; ENSG00000142657; Tissue enhanced (bone marrow, esophagus).
DR MIM; 172200; gene.
DR neXtProt; NX_P52209; -.
DR OpenTargets; ENSG00000142657; -.
DR PharmGKB; PA33229; -.
DR VEuPathDB; HostDB:ENSG00000142657; -.
DR eggNOG; KOG2653; Eukaryota.
DR GeneTree; ENSGT00390000009023; -.
DR HOGENOM; CLU_024540_4_2_1; -.
DR InParanoid; P52209; -.
DR OMA; VIMVKAG; -.
DR OrthoDB; 847823at2759; -.
DR PhylomeDB; P52209; -.
DR TreeFam; TF300386; -.
DR BioCyc; MetaCyc:HS06949-MON; -.
DR BRENDA; 1.1.1.44; 2681.
DR PathwayCommons; P52209; -.
DR Reactome; R-HSA-71336; Pentose phosphate pathway.
DR Reactome; R-HSA-9759194; Nuclear events mediated by NFE2L2.
DR SABIO-RK; P52209; -.
DR SignaLink; P52209; -.
DR SIGNOR; P52209; -.
DR UniPathway; UPA00115; UER00410.
DR BioGRID-ORCS; 5226; 640 hits in 1093 CRISPR screens.
DR ChiTaRS; PGD; human.
DR EvolutionaryTrace; P52209; -.
DR GenomeRNAi; 5226; -.
DR Pharos; P52209; Tchem.
DR PRO; PR:P52209; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P52209; protein.
DR Bgee; ENSG00000142657; Expressed in lower esophagus mucosa and 190 other tissues.
DR ExpressionAtlas; P52209; baseline and differential.
DR Genevisible; P52209; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IBA:GO_Central.
DR GO; GO:0004616; F:phosphogluconate dehydrogenase (decarboxylating) activity; ISS:UniProtKB.
DR GO; GO:0046177; P:D-gluconate catabolic process; IBA:GO_Central.
DR GO; GO:0019322; P:pentose biosynthetic process; IEA:Ensembl.
DR GO; GO:0006098; P:pentose-phosphate shunt; ISS:UniProtKB.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IDA:UniProtKB.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR006114; 6PGDH_C.
DR InterPro; IPR006113; 6PGDH_Gnd/GntZ.
DR InterPro; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR006184; 6PGdom_BS.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006183; Pgluconate_DH.
DR PANTHER; PTHR11811; PTHR11811; 1.
DR Pfam; PF00393; 6PGD; 1.
DR Pfam; PF03446; NAD_binding_2; 1.
DR PIRSF; PIRSF000109; 6PGD; 1.
DR PRINTS; PR00076; 6PGDHDRGNASE.
DR SMART; SM01350; 6PGD; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00873; gnd; 1.
DR PROSITE; PS00461; 6PGD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Gluconate utilization; NADP; Oxidoreductase; Pentose shunt; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..483
FT /note="6-phosphogluconate dehydrogenase, decarboxylating"
FT /id="PRO_0000090063"
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 10..15
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 33..35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 75..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 103
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 103
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 129..131
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 187..188
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 478..481
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 38
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCD0"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCD0"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCD0"
FT MOD_RES 309
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055767"
FT VARIANT 268
FT /note="A -> S (in dbSNP:rs11547610)"
FT /id="VAR_048104"
FT CONFLICT 118
FT /note="A -> G (in Ref. 1; AAA75302)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="A -> P (in Ref. 1; AAA75302)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:4GWG"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:4GWG"
FT TURN 45..49
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:4GWG"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4GWG"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:4GWG"
FT STRAND 122..130
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 131..137
FT /evidence="ECO:0007829|PDB:4GWG"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:4GWG"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2JKV"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:4GWG"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:5UQ9"
FT HELIX 179..207
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:4GWG"
FT TURN 224..228
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:4GWG"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 265..274
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 316..349
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:4GWG"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:5UQ9"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 393..416
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:4GWG"
FT HELIX 440..451
FT /evidence="ECO:0007829|PDB:4GWG"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:4GWG"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:4GWG"
SQ SEQUENCE 483 AA; 53140 MW; 6CEFC0077D1283E3 CRC64;
MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE
MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG
ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG
HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL
KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA
SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL
MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM
PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS
YNA
