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   24-JAN-2024, entry version 217.
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 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; 29.
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   EPD; P07451; -.
DR   MassIVE; P07451; -.
DR   PaxDb; 9606-ENSP00000285381; -.
DR   PeptideAtlas; P07451; -.
DR   ProteomicsDB; 52004; -.
DR   Antibodypedia; 3326; 498 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   AGR; HGNC:1374; -.
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; WHELYPN; -.
DR   OrthoDB; 49814at2759; -.
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; 11 hits in 1156 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 141 other cell types or tissues.
DR   ExpressionAtlas; P07451; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0016151; F:nickel cation binding; 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   CDD; cd03119; alpha_CA_I_II_III_XIII; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 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   PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF127; CARBONIC ANHYDRASE 3; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   UCD-2DPAGE; P07451; -.
DR   Genevisible; P07451; HS.
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
//