ISAHY_ROSAI
ID ISAHY_ROSAI Reviewed; 263 AA.
AC A0NLY7;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Isatin hydrolase {ECO:0000303|PubMed:24917679};
DE EC=3.5.2.20 {ECO:0000269|PubMed:24917679};
DE AltName: Full=Isatin amidohydrolase {ECO:0000305};
DE AltName: Full=Isatin hydrolase isoform b {ECO:0000303|PubMed:24917679};
DE Short=IH-b {ECO:0000303|PubMed:24917679};
GN ORFNames=SIAM614_09648 {ECO:0000312|EMBL:EAV46082.1};
OS Roseibium aggregatum (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC
OS 16684 / NCIMB 2208 / IAM 12614 / B1) (Stappia aggregata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Roseibium.
OX NCBI_TaxID=384765;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM
RC 12614 / B1 {ECO:0000312|Proteomes:UP000004848};
RA King G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP MANGANESE ION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF SER-225, ACTIVITY REGULATION, COFACTOR, ACTIVE SITE, AND
RP SUBUNIT.
RC STRAIN=ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM
RC 12614 / B1;
RX PubMed=24917679; DOI=10.1074/jbc.m114.568824;
RA Bjerregaard-Andersen K., Sommer T., Jensen J.K., Jochimsen B., Etzerodt M.,
RA Morth J.P.;
RT "A proton wire and water channel revealed in the crystal structure of
RT isatin hydrolase.";
RL J. Biol. Chem. 289:21351-21359(2014).
CC -!- FUNCTION: Involved in the degradation of the plant hormone indole-3-
CC acetic acid (IAA). Catalyzes the hydrolysis of the cyclic amide bond
CC (lactam) of isatin (1H-indole-2,3-dione) to yield isatinate (2-(2-
CC aminophenyl)-2-oxoacetate). {ECO:0000269|PubMed:24917679}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + isatin = H(+) + isatinate; Xref=Rhea:RHEA:43232,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27539,
CC ChEBI:CHEBI:82904; EC=3.5.2.20;
CC Evidence={ECO:0000269|PubMed:24917679};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:24917679};
CC Note=Binds 1 manganese ion per subunit. {ECO:0000269|PubMed:24917679};
CC -!- ACTIVITY REGULATION: Inhibited by thioisatinate.
CC {ECO:0000269|PubMed:24917679}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.8 uM for isatin {ECO:0000269|PubMed:24917679};
CC Vmax=0.24 umol/sec/mg enzyme {ECO:0000269|PubMed:24917679};
CC Note=kcat is 24 sec(-1) for isatin as substrate.
CC {ECO:0000269|PubMed:24917679};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24917679}.
CC -!- SIMILARITY: Belongs to the Cyclase 1 superfamily. {ECO:0000305}.
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DR EMBL; AAUW01000001; EAV46082.1; -; Genomic_DNA.
DR RefSeq; WP_006931350.1; NZ_AAUW01000001.1.
DR PDB; 4J0N; X-ray; 2.25 A; A/B=1-263.
DR PDB; 4M8D; X-ray; 1.90 A; A/B/C/D/E/F/G/H/I/J/K/L=1-263.
DR PDBsum; 4J0N; -.
DR PDBsum; 4M8D; -.
DR AlphaFoldDB; A0NLY7; -.
DR SMR; A0NLY7; -.
DR eggNOG; COG1878; Bacteria.
DR OrthoDB; 831439at2; -.
DR BRENDA; 3.5.2.20; 9995.
DR Proteomes; UP000004848; Unassembled WGS sequence.
DR GO; GO:0004061; F:arylformamidase activity; IEA:InterPro.
DR GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:InterPro.
DR Gene3D; 3.50.30.50; -; 1.
DR InterPro; IPR007325; KFase/CYL.
DR InterPro; IPR037175; KFase_sf.
DR PANTHER; PTHR31118; PTHR31118; 1.
DR Pfam; PF04199; Cyclase; 1.
DR SUPFAM; SSF102198; SSF102198; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Manganese; Metal-binding.
FT CHAIN 1..263
FT /note="Isatin hydrolase"
FT /id="PRO_0000444711"
FT ACT_SITE 83
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:24917679"
FT BINDING 62..66
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:24917679"
FT BINDING 73
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24917679,
FT ECO:0007744|PDB:4J0N, ECO:0007744|PDB:4M8D"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24917679,
FT ECO:0007744|PDB:4J0N, ECO:0007744|PDB:4M8D"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24917679,
FT ECO:0007744|PDB:4J0N, ECO:0007744|PDB:4M8D"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24917679,
FT ECO:0007744|PDB:4M8D"
FT MUTAGEN 225
FT /note="S->A: No effect on the affinity for isatin and on
FT the catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24917679"
FT MUTAGEN 225
FT /note="S->C: 2-fold decrease of the affinity for isatin and
FT 4-fold increase of the catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:24917679"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:4M8D"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 60..73
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4M8D"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:4M8D"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:4M8D"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:4M8D"
SQ SEQUENCE 263 AA; 28053 MW; 86C412752BD8EBE2 CRC64;
MSAQSALSGL GAKLLSGEVE VVDCTGVLGP NTPILQLPPD FAKNTPKVEI HKISEYDSDG
PFFAWNWMVL GEHSGTHFDA PHHWITGKDY SDGFTDTLDV QRLIAPVNVI DCSKESAADP
DFLLTADLIK AWEAEHGEIG AGEWVVMRTD WDKRAGDEAA FLNADETGPH SPGPTPDAIE
YLLSKKIVGW GSQCIGTDAG QAGGMEPPFP AHNLLHRDNC FGLASLANLD KLPAKGAILI
AAPLKIERGT GSPIRALALV PKA
