CAH3_HUMAN
ID CAH3_HUMAN Reviewed; 260 AA.
AC P07451; B2R867; B3KUC8; O60842;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Carbonic anhydrase 3 {ECO:0000305};
DE EC=4.2.1.1;
DE AltName: Full=Carbonate dehydratase III {ECO:0000303|PubMed:3099285};
DE AltName: Full=Carbonic anhydrase III {ECO:0000303|PubMed:3099285};
DE Short=CA-III {ECO:0000303|PubMed:3099285};
GN Name=CA3 {ECO:0000303|PubMed:9651514, ECO:0000312|HGNC:HGNC:1374};
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], AND TISSUE SPECIFICITY.
RX PubMed=3086182; DOI=10.1016/0378-1119(86)90103-4;
RA Lloyd J., McMillan S., Hopkinson D., Edwards Y.H.;
RT "Nucleotide sequence and derived amino acid sequence of a cDNA encoding
RT human muscle carbonic anhydrase.";
RL Gene 41:233-239(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=3099285; DOI=10.1073/pnas.83.24.9571;
RA Wade R., Gunning P., Eddy R., Shows T., Kedes L.;
RT "Nucleotide sequence, tissue-specific expression, and chromosome location
RT of human carbonic anhydrase III: the human CAIII gene is located on the
RT same chromosome as the closely linked CAI and CAII genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9571-9575(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-31.
RC TISSUE=Pericardium, and Skeletal muscle;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-31.
RA Mural R.J., Istrail S., Sutton G.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], AND VARIANT ILE-31.
RC TISSUE=Muscle;
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 PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2824285; DOI=10.1101/gad.1.6.594;
RA Lloyd J., Brownson C., Tweedie S., Charlton J., Edwards Y.H.;
RT "Human muscle carbonic anhydrase: gene structure and DNA methylation
RT patterns in fetal and adult tissues.";
RL Genes Dev. 1:594-602(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11, AND DEVELOPMENTAL STAGE.
RX PubMed=9651514; DOI=10.1016/s0378-1119(98)00201-7;
RA Sowden J., Smith H., Morrison K., Edwards Y.;
RT "Sequence comparisons and functional studies of the proximal promoter of
RT the carbonic anhydrase 3 (CA3) gene.";
RL Gene 214:157-165(1998).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038;
RA Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A.,
RA Muehlschlegel F.A., Supuran C.T.;
RT "A thiabendazole sulfonamide shows potent inhibitory activity against
RT mammalian and nematode alpha-carbonic anhydrases.";
RL Bioorg. Med. Chem. Lett. 19:1371-1375(2009).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=19206230; DOI=10.1021/ja809683v;
RA Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A.,
RA Quinn R.J., Supuran C.T.;
RT "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new
RT class of suicide inhibitors.";
RL J. Am. Chem. Soc. 131:3057-3062(2009).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND ACTIVITY REGULATION.
RX PubMed=18618712; DOI=10.1002/prot.22144;
RA Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A.,
RA Pedone C., Scozzafava A., Supuran C.T., De Simone G.;
RT "Crystal structure of human carbonic anhydrase XIII and its complex with
RT the inhibitor acetazolamide.";
RL Proteins 74:164-175(2009).
RN [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-260 IN COMPLEX WITH ZINC ION,
RP MUTAGENESIS OF PHE-197, ACTIVATION BY IMIDAZOLE AND HISTIDYLHISTIDINE,
RP ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=16042381; DOI=10.1021/bi050610h;
RA Duda D.M., Tu C., Fisher S.Z., An H., Yoshioka C., Govindasamy L.,
RA Laipis P.J., Agbandje-McKenna M., Silverman D.N., McKenna R.;
RT "Human carbonic anhydrase III: structural and kinetic study of catalysis
RT and proton transfer.";
RL Biochemistry 44:10046-10053(2005).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-260 IN COMPLEX WITH ZINC ION,
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-64 AND ARG-67, AND
RP COFACTOR.
RX PubMed=17427958; DOI=10.1002/prot.21403;
RA Elder I., Fisher Z., Laipis P.J., Tu C., McKenna R., Silverman D.N.;
RT "Structural and kinetic analysis of proton shuttle residues in the active
RT site of human carbonic anhydrase III.";
RL Proteins 68:337-343(2007).
CC -!- FUNCTION: Reversible hydration of carbon dioxide.
CC {ECO:0000269|PubMed:17427958, ECO:0000269|PubMed:18618712}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:17427958,
CC ECO:0000269|PubMed:18618712};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16042381, ECO:0000269|PubMed:17427958};
CC -!- ACTIVITY REGULATION: Activated by proton donors such as imidazole and
CC the dipeptide histidylhistidine (PubMed:16042381). Inhibited by
CC coumarins and sulfonamide derivatives such as acetazolamide
CC (PubMed:18618712, PubMed:19186056, PubMed:19206230).
CC {ECO:0000269|PubMed:16042381, ECO:0000269|PubMed:18618712,
CC ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=52.0 mM for CO(2) {ECO:0000269|PubMed:18618712};
CC -!- INTERACTION:
CC P07451; P37235: HPCAL1; NbExp=3; IntAct=EBI-12208965, EBI-749311;
CC P07451; Q9BS40: LXN; NbExp=3; IntAct=EBI-12208965, EBI-1044504;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18618712}.
CC -!- TISSUE SPECIFICITY: Muscle specific. {ECO:0000269|PubMed:3086182,
CC ECO:0000269|PubMed:3099285}.
CC -!- DEVELOPMENTAL STAGE: At 6 weeks gestation, transcripts accumulate at
CC low levels in the somites and at high levels throughout the notochord.
CC As gestation continues, CA3 becomes abundant in all developing muscle
CC masses and continues at high to moderate levels in the notochord.
CC {ECO:0000269|PubMed:9651514}.
CC -!- PTM: S-thiolated both by thiol-disulfide exchange with glutathione
CC disulfide and by oxyradical-initiated S-thiolation with reduced
CC glutathione. {ECO:0000250|UniProtKB:P14141}.
CC -!- PTM: S-glutathionylated in hepatocytes under oxidative stress.
CC {ECO:0000250|UniProtKB:P14141}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; M29458; AAA52293.1; -; Genomic_DNA.
DR EMBL; M29452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK096880; BAG53390.1; -; mRNA.
DR EMBL; AK313254; BAG36064.1; -; mRNA.
DR EMBL; CH471068; EAW87133.1; -; Genomic_DNA.
DR EMBL; BC004897; AAH04897.1; -; mRNA.
DR EMBL; AJ006473; CAA07056.1; -; Genomic_DNA.
DR CCDS; CCDS6238.1; -.
DR PIR; A26658; CRHU3.
DR RefSeq; NP_005172.1; NM_005181.3.
DR PDB; 1Z93; X-ray; 2.10 A; A=1-260.
DR PDB; 1Z97; X-ray; 2.10 A; A=1-260.
DR PDB; 2HFW; X-ray; 2.50 A; A=1-259.
DR PDB; 3UYN; X-ray; 2.60 A; A=1-260.
DR PDB; 3UYQ; X-ray; 1.70 A; A=1-260.
DR PDBsum; 1Z93; -.
DR PDBsum; 1Z97; -.
DR PDBsum; 2HFW; -.
DR PDBsum; 3UYN; -.
DR PDBsum; 3UYQ; -.
DR AlphaFoldDB; P07451; -.
DR SMR; P07451; -.
DR BioGRID; 107216; 28.
DR IntAct; P07451; 2.
DR STRING; 9606.ENSP00000285381; -.
DR BindingDB; P07451; -.
DR ChEMBL; CHEMBL2885; -.
DR DrugBank; DB00819; Acetazolamide.
DR DrugBank; DB00562; Benzthiazide.
DR DrugBank; DB01194; Brinzolamide.
DR DrugBank; DB00482; Celecoxib.
DR DrugBank; DB00606; Cyclothiazide.
DR DrugBank; DB01144; Diclofenamide.
DR DrugBank; DB00869; Dorzolamide.
DR DrugBank; DB08846; Ellagic acid.
DR DrugBank; DB00311; Ethoxzolamide.
DR DrugBank; DB00703; Methazolamide.
DR DrugBank; DB12418; Saccharin.
DR DrugBank; DB00391; Sulpiride.
DR DrugBank; DB00273; Topiramate.
DR DrugBank; DB00580; Valdecoxib.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; P07451; -.
DR GlyGen; P07451; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P07451; -.
DR PhosphoSitePlus; P07451; -.
DR BioMuta; CA3; -.
DR DMDM; 134047703; -.
DR UCD-2DPAGE; P07451; -.
DR EPD; P07451; -.
DR MassIVE; P07451; -.
DR PaxDb; P07451; -.
DR PeptideAtlas; P07451; -.
DR PRIDE; P07451; -.
DR ProteomicsDB; 52004; -.
DR Antibodypedia; 3326; 454 antibodies from 35 providers.
DR DNASU; 761; -.
DR Ensembl; ENST00000285381.3; ENSP00000285381.2; ENSG00000164879.7.
DR GeneID; 761; -.
DR KEGG; hsa:761; -.
DR MANE-Select; ENST00000285381.3; ENSP00000285381.2; NM_005181.4; NP_005172.1.
DR CTD; 761; -.
DR DisGeNET; 761; -.
DR GeneCards; CA3; -.
DR HGNC; HGNC:1374; CA3.
DR HPA; ENSG00000164879; Tissue enriched (skeletal).
DR MIM; 114750; gene.
DR neXtProt; NX_P07451; -.
DR OpenTargets; ENSG00000164879; -.
DR PharmGKB; PA25990; -.
DR VEuPathDB; HostDB:ENSG00000164879; -.
DR eggNOG; KOG0382; Eukaryota.
DR GeneTree; ENSGT00940000159435; -.
DR HOGENOM; CLU_039326_2_1_1; -.
DR InParanoid; P07451; -.
DR OMA; ERWHENY; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P07451; -.
DR TreeFam; TF316425; -.
DR BRENDA; 4.2.1.1; 2681.
DR PathwayCommons; P07451; -.
DR Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
DR SignaLink; P07451; -.
DR BioGRID-ORCS; 761; 10 hits in 1070 CRISPR screens.
DR ChiTaRS; CA3; human.
DR EvolutionaryTrace; P07451; -.
DR GeneWiki; Carbonic_anhydrase_III,_muscle_specific; -.
DR GenomeRNAi; 761; -.
DR Pharos; P07451; Tclin.
DR PRO; PR:P07451; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P07451; protein.
DR Bgee; ENSG00000164879; Expressed in skeletal muscle tissue of rectus abdominis and 139 other tissues.
DR ExpressionAtlas; P07451; baseline and differential.
DR Genevisible; P07451; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central.
DR GO; GO:0016151; F:nickel cation binding; IEA:Ensembl.
DR GO; GO:0016791; F:phosphatase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR Gene3D; 3.10.200.10; -; 1.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR InterPro; IPR018441; Carbonic_anhydrase_CA3.
DR PANTHER; PTHR18952; PTHR18952; 1.
DR PANTHER; PTHR18952:SF127; PTHR18952:SF127; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; SSF51069; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Glutathionylation; Lyase;
KW Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07450"
FT CHAIN 2..260
FT /note="Carbonic anhydrase 3"
FT /id="PRO_0000077426"
FT DOMAIN 3..259
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REGION 64..67
FT /note="Involved in proton transfer"
FT /evidence="ECO:0000269|PubMed:17427958"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16042381,
FT ECO:0000269|PubMed:17427958"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16042381,
FT ECO:0000269|PubMed:17427958"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16042381,
FT ECO:0000269|PubMed:17427958"
FT BINDING 198..199
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00918"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P07450"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 129
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16015"
FT MOD_RES 182
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 187
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14141"
FT VARIANT 31
FT /note="V -> I (in dbSNP:rs20571)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_016180"
FT MUTAGEN 64
FT /note="K->H: Enhanced proton transfer in catalysis."
FT /evidence="ECO:0000269|PubMed:17427958"
FT MUTAGEN 67
FT /note="R->H: Enhanced proton transfer in catalysis."
FT /evidence="ECO:0000269|PubMed:17427958"
FT MUTAGEN 197
FT /note="F->L: Enhanced activity by at least 10-fold."
FT /evidence="ECO:0000269|PubMed:16042381"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:3UYQ"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:3UYQ"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3UYQ"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2HFW"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:3UYQ"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:3UYQ"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3UYQ"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 139..151
FT /evidence="ECO:0007829|PDB:3UYQ"
FT HELIX 154..160
FT /evidence="ECO:0007829|PDB:3UYQ"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3UYQ"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3UYQ"
FT HELIX 219..225
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:3UYQ"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3UYQ"
SQ SEQUENCE 260 AA; 29557 MW; A305334167233FCF CRC64;
MAKEWGYASH NGPDHWHELF PNAKGENQSP VELHTKDIRH DPSLQPWSVS YDGGSAKTIL
NNGKTCRVVF DDTYDRSMLR GGPLPGPYRL RQFHLHWGSS DDHGSEHTVD GVKYAAELHL
VHWNPKYNTF KEALKQRDGI AVIGIFLKIG HENGEFQIFL DALDKIKTKG KEAPFTKFDP
SCLFPACRDY WTYQGSFTTP PCEECIVWLL LKEPMTVSSD QMAKLRSLLS SAENEPPVPL
VSNWRPPQPI NNRVVRASFK
