NHAB_PSETH
ID NHAB_PSETH Reviewed; 233 AA.
AC Q7SID3;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Cobalt-containing nitrile hydratase subunit beta;
DE Short=L-NHase;
DE Short=L-nitrilase;
DE EC=4.2.1.84;
OS Pseudonocardia thermophila.
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Pseudonocardia.
OX NCBI_TaxID=1848 {ECO:0000312|PDB:1IRE};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-7, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=ATCC 19285 / DSM 43832 / JCM 3095 / CBS 277.66 / NBRC 15559 / NCIMB
RC 10079 / NRRL B-1978;
RA Yamaki T., Oikawa T., Ito K., Nakamura T.;
RT "Cloning and sequencing of a nitrile hydratase gene from Pseudonocardia
RT thermophila JCM3095.";
RL J. Ferment. Bioeng. 83:474-477(1997).
RN [2] {ECO:0000312|PDB:1IRE}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-229.
RC STRAIN=ATCC 19285 / DSM 43832 / JCM 3095 / CBS 277.66 / NBRC 15559 / NCIMB
RC 10079 / NRRL B-1978;
RX PubMed=11700034; DOI=10.1006/bbrc.2001.5897;
RA Miyanaga A., Fushinobu S., Ito K., Wakagi T.;
RT "Crystal structure of cobalt-containing nitrile hydratase.";
RL Biochem. Biophys. Res. Commun. 288:1169-1174(2001).
CC -!- FUNCTION: NHase catalyzes the hydration of various nitrile compounds to
CC the corresponding amides. {ECO:0000305}.
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 Evidence={ECO:0000269|Ref.1, ECO:0000305};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.;
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000269|PubMed:11700034}.
CC -!- INTERACTION:
CC Q7SID3; Q7SID2; NbExp=5; IntAct=EBI-1032285, EBI-1032292;
CC -!- BIOTECHNOLOGY: Industrial production of acrylamide is now being
CC developed using some of these enzymes. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nitrile hydratase subunit beta family.
CC {ECO:0000305}.
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DR RefSeq; WP_073455623.1; NZ_FRAP01000003.1.
DR PDB; 1IRE; X-ray; 1.80 A; B=1-228.
DR PDB; 1UGP; X-ray; 1.63 A; B=1-226.
DR PDB; 1UGQ; X-ray; 2.00 A; B=1-228.
DR PDB; 1UGR; X-ray; 1.80 A; B=1-228.
DR PDB; 1UGS; X-ray; 2.00 A; B=1-228.
DR PDB; 3VYH; X-ray; 1.63 A; B=1-233.
DR PDB; 4OB0; X-ray; 1.20 A; B=1-233.
DR PDB; 4OB1; X-ray; 1.63 A; B=1-233.
DR PDB; 4OB2; X-ray; 1.52 A; B=1-233.
DR PDB; 4OB3; X-ray; 1.92 A; B=1-233.
DR PDB; 7SJZ; X-ray; 1.85 A; B=1-233.
DR PDBsum; 1IRE; -.
DR PDBsum; 1UGP; -.
DR PDBsum; 1UGQ; -.
DR PDBsum; 1UGR; -.
DR PDBsum; 1UGS; -.
DR PDBsum; 3VYH; -.
DR PDBsum; 4OB0; -.
DR PDBsum; 4OB1; -.
DR PDBsum; 4OB2; -.
DR PDBsum; 4OB3; -.
DR PDBsum; 7SJZ; -.
DR AlphaFoldDB; Q7SID3; -.
DR SMR; Q7SID3; -.
DR IntAct; Q7SID3; 1.
DR STRING; 1848.SAMN05443637_10360; -.
DR BRENDA; 4.2.1.84; 5208.
DR EvolutionaryTrace; Q7SID3; -.
DR GO; GO:0080109; F:indole-3-acetonitrile nitrile hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0018822; F:nitrile hydratase activity; IDA:UniProtKB.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0050899; P:nitrile catabolic process; IDA:UniProtKB.
DR Gene3D; 1.10.472.20; -; 1.
DR InterPro; IPR042262; CN_hydtase_beta_C.
DR InterPro; IPR024690; CN_hydtase_beta_dom.
DR InterPro; IPR008990; Elect_transpt_acc-like_dom_sf.
DR InterPro; IPR003168; Nitrile_hydratase_bsu.
DR Pfam; PF02211; NHase_beta; 1.
DR PIRSF; PIRSF001427; NHase_beta; 1.
DR SUPFAM; SSF50090; SSF50090; 1.
DR TIGRFAMs; TIGR03888; nitrile_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lyase.
FT CHAIN 1..233
FT /note="Cobalt-containing nitrile hydratase subunit beta"
FT /id="PRO_0000186830"
FT HELIX 28..42
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:4OB0"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:4OB0"
FT STRAND 166..176
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 179..182
FT /evidence="ECO:0007829|PDB:4OB0"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:4OB0"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1UGP"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:4OB0"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:4OB0"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4OB0"
SQ SEQUENCE 233 AA; 26550 MW; ECA070F18BCE62F0 CRC64;
MNGVYDVGGT DGLGPINRPA DEPVFRAEWE KVAFAMFPAT FRAGFMGLDE FRFGIEQMNP
AEYLESPYYW HWIRTYIHHG VRTGKIDLEE LERRTQYYRE NPDAPLPEHE QKPELIEFVN
QAVYGGLPAS REVDRPPKFK EGDVVRFSTA SPKGHARRAR YVRGKTGTVV KHHGAYIYPD
TAGNGLGECP EHLYTVRFTA QELWGPEGDP NSSVYYDCWE PYIELVDTKA AAA
