ID   NHAAB_MONBE             Reviewed;         496 AA.
AC   A9V2C1;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Probable nitrile hydratase;
DE            Short=NHase;
DE            Short=Nitrilase;
DE            EC=4.2.1.84;
GN   ORFNames=37534;
OS   Monosiga brevicollis (Choanoflagellate).
OC   Eukaryota; Choanoflagellata; Craspedida; Salpingoecidae; Monosiga.
OX   NCBI_TaxID=81824;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX1 / ATCC 50154;
RX   PubMed=18273011; DOI=10.1038/nature06617;
RG   JGI Sequencing;
RA   King N., Westbrook M.J., Young S.L., Kuo A., Abedin M., Chapman J.,
RA   Fairclough S., Hellsten U., Isogai Y., Letunic I., Marr M., Pincus D.,
RA   Putnam N., Rokas A., Wright K.J., Zuzow R., Dirks W., Good M.,
RA   Goodstein D., Lemons D., Li W., Lyons J.B., Morris A., Nichols S.,
RA   Richter D.J., Salamov A., Bork P., Lim W.A., Manning G., Miller W.T.,
RA   McGinnis W., Shapiro H., Tjian R., Grigoriev I.V., Rokhsar D.;
RT   "The genome of the choanoflagellate Monosiga brevicollis and the origin of
RT   metazoans.";
RL   Nature 451:783-788(2008).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=19096720; DOI=10.1371/journal.pone.0003976;
RA   Foerstner K.U., Doerks T., Muller J., Raes J., Bork P.;
RT   "A nitrile hydratase in the eukaryote Monosiga brevicollis.";
RL   PLoS ONE 3:E3976-E3976(2008).
CC   -!- FUNCTION: NHase catalyzes the hydration of various nitrile compounds to
CC       the corresponding amides. Industrial production of acrylamide is now
CC       being developed using some of the enzymes of this class (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aliphatic amide = a nitrile + H2O; Xref=Rhea:RHEA:12673,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:18379, ChEBI:CHEBI:65285; EC=4.2.1.84;
CC   -!- COFACTOR:
CC       Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250};
CC   -!- PTM: Oxidation on Cys-403 is essential for the activity. {ECO:0000250}.
CC   -!- PTM: Oxidation on Cys-405 stabilizes the Fe-NO ligand coordinated in
CC       the inactive form. {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the nitrile hydratase
CC       subunit alpha family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the nitrile hydratase
CC       subunit beta family. {ECO:0000305}.
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DR   EMBL; CH991555; EDQ88232.1; -; Genomic_DNA.
DR   RefSeq; XP_001746825.1; XM_001746773.1.
DR   AlphaFoldDB; A9V2C1; -.
DR   SMR; A9V2C1; -.
DR   STRING; 81824.XP_001746825.1; -.
DR   EnsemblProtists; EDQ88232; EDQ88232; MONBRDRAFT_37534.
DR   GeneID; 5892148; -.
DR   KEGG; mbr:MONBRDRAFT_37534; -.
DR   eggNOG; ENOG502S164; Eukaryota.
DR   InParanoid; A9V2C1; -.
DR   OMA; LCSCYPA; -.
DR   BRENDA; 4.2.1.84; 7932.
DR   Proteomes; UP000001357; Unassembled WGS sequence.
DR   GO; GO:0080109; F:indole-3-acetonitrile nitrile hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.472.20; -; 1.
DR   Gene3D; 3.90.330.10; -; 1.
DR   InterPro; IPR036648; CN_Hdrase_a/SCN_Hdrase_g_sf.
DR   InterPro; IPR004232; CN_Hdrtase_a/SCN_Hdrlase_g.
DR   InterPro; IPR042262; CN_hydtase_beta_C.
DR   InterPro; IPR024690; CN_hydtase_beta_dom.
DR   InterPro; IPR008990; Elect_transpt_acc-like_dom_sf.
DR   Pfam; PF02979; NHase_alpha; 1.
DR   Pfam; PF02211; NHase_beta; 2.
DR   SUPFAM; SSF50090; SSF50090; 1.
DR   SUPFAM; SSF56209; SSF56209; 1.
PE   3: Inferred from homology;
KW   Iron; Lyase; Metal-binding; Oxidation; Reference proteome.
FT   CHAIN           1..496
FT                   /note="Probable nitrile hydratase"
FT                   /id="PRO_0000389131"
FT   REGION          229..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..261
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         400
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   BINDING         403
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   BINDING         404
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   BINDING         405
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         403
FT                   /note="Cysteine sulfinic acid (-SO2H)"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         405
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   496 AA;  55604 MW;  D59041CBAAAB3949 CRC64;
     MHLFTYDLHH DVGGAENMLR LPLDRHERDY LPWERHIHAL VVLLVKQGRM SVDELRRGVE
     GLPSSLAEQA SYYEKWGLSV SRILTEKGTV SGHELEQGFL GVPTTDLPQV PRFQVGQRVM
     VRPFGTTFAY RQPHLRVPGY VHGAVGTIVE LPGLFQDPMT GAYGERGTAQ PLYRVAFSHR
     ALWPEGAAHA EPGELEDGVV VDVSQPWLEA LSEADYAQRL ATLHRVAFTP DSNPPQAHKH
     HHHRHHHDHH HHHHHHHAMH AEHEAHTHDT RYGTEQAAVA KEAALDFPYQ PWCEALVQTL
     TRRGVVRSDE LHATLASLDA LQNSGAGPQL VARAWSDAAF AEWLLTDAAA AAESLAIRTT
     NYDADPASAE RVGGHRLFSH NHTELRVVAN TDTVHNLVCC TLCSCYPTAI LGLSPPWYKS
     KVFRARAVRE PRRLLREEFG LVLPEARGIR VHDSTADLRY MVLPQRPQGT EGWSEEHLRT
     IVTRDSLLGT AVPRVD