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 27-MAR-2024, entry version 216. 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; 175. DR IntAct; P52209; 38. 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-2711; -. DR CPTAC; CPTAC-560; -. DR CPTAC; CPTAC-561; -. DR EPD; P52209; -. DR jPOST; P52209; -. DR MassIVE; P52209; -. DR MaxQB; P52209; -. DR PaxDb; 9606-ENSP00000270776; -. DR PeptideAtlas; P52209; -. DR PRIDE; P52209; -. DR ProteomicsDB; 4884; -. DR ProteomicsDB; 56472; -. [P52209-1] DR Pumba; P52209; -. DR TopDownProteomics; P52209-1; -. [P52209-1] DR Antibodypedia; 27894; 380 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 AGR; HGNC:8891; -. 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; CVTHVGP; -. DR OrthoDB; 3013545at2759; -. DR PhylomeDB; P52209; -. DR TreeFam; TF300386; -. DR BioCyc; MetaCyc:HS06949-MONOMER; -. DR BRENDA; 1.1.1.44; 2681. DR PathwayCommons; P52209; -. DR Reactome; R-HSA-71336; Pentose phosphate pathway. DR Reactome; R-HSA-9818028; NFE2L2 regulates pentose phosphate pathway genes. DR SABIO-RK; P52209; -. DR SignaLink; P52209; -. DR SIGNOR; P52209; -. DR UniPathway; UPA00115; UER00410. DR BioGRID-ORCS; 5226; 675 hits in 1175 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 192 other cell types or tissues. DR ExpressionAtlas; P52209; baseline and differential. 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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 NCBIfam; TIGR00873; gnd; 1. DR PANTHER; PTHR11811; 6-PHOSPHOGLUCONATE DEHYDROGENASE; 1. DR PANTHER; PTHR11811:SF50; 6-PHOSPHOGLUCONATE DEHYDROGENASE, DECARBOXYLATING; 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; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00461; 6PGD; 1. DR Genevisible; P52209; HS. 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 //