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P13449

- NHAB_RHOER

UniProt

P13449 - NHAB_RHOER

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Protein

Nitrile hydratase subunit beta

Gene

nthB

Organism
Rhodococcus erythropolis (Arthrobacter picolinophilus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

NHase catalyzes the hydration of various nitrile compounds to the corresponding amides.

Catalytic activityi

An aliphatic amide = a nitrile + H2O.

GO - Molecular functioni

  1. indole-3-acetonitrile nitrile hydratase activity Source: UniProtKB-EC
  2. transition metal ion binding Source: InterPro

GO - Biological processi

  1. nitrogen compound metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

SABIO-RKP13449.

Names & Taxonomyi

Protein namesi
Recommended name:
Nitrile hydratase subunit beta (EC:4.2.1.84)
Short name:
NHase
Short name:
Nitrilase
Gene namesi
Name:nthB
Synonyms:nha2
OrganismiRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifieri1833 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Pathology & Biotechi

Biotechnological usei

Industrial production of acrylamide is now being developed using some of these enzymes.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Nitrile hydratase subunit betaPRO_0000186831Add
BLAST

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta chain.

Protein-protein interaction databases

DIPiDIP-6076N.

Structurei

Secondary structure

1
212
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni31 – 344Combined sources
Helixi35 – 4511Combined sources
Helixi52 – 609Combined sources
Helixi64 – 696Combined sources
Helixi72 – 8615Combined sources
Helixi92 – 998Combined sources
Beta strandi128 – 1314Combined sources
Helixi144 – 1463Combined sources
Beta strandi150 – 1567Combined sources
Helixi164 – 1674Combined sources
Turni168 – 1703Combined sources
Beta strandi179 – 1857Combined sources
Helixi186 – 1905Combined sources
Beta strandi197 – 2048Combined sources
Helixi205 – 2073Combined sources
Beta strandi208 – 2103Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHJX-ray2.65B/D/F/H1-212[»]
2AHJX-ray1.70B/D1-212[»]
2CYZX-ray1.55B1-212[»]
2CZ0X-ray1.50B1-212[»]
2CZ1X-ray1.39B1-212[»]
2CZ6X-ray1.50B1-212[»]
2CZ7X-ray1.80B1-212[»]
2D0QX-ray1.65B1-212[»]
2QDYX-ray1.30B1-212[»]
2ZCFX-ray1.43B1-212[»]
2ZPBX-ray1.30B1-212[»]
2ZPEX-ray1.48B1-212[»]
2ZPFX-ray1.48B1-212[»]
2ZPGX-ray1.39B1-212[»]
2ZPHX-ray1.59B1-212[»]
2ZPIX-ray1.49B1-212[»]
3A8GX-ray1.11B1-212[»]
3A8HX-ray1.66B1-212[»]
3A8LX-ray1.63B1-212[»]
3A8MX-ray1.32B1-212[»]
3A8OX-ray1.47B1-212[»]
ProteinModelPortaliP13449.
SMRiP13449. Positions 1-212.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13449.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR024690. CN_hydtase_beta_dom.
IPR008990. Elect_transpt_acc-like_dom.
IPR003168. Nitrile_hydratase_bsu.
[Graphical view]
PfamiPF02211. NHase_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF001427. NHase_beta. 1 hit.
SUPFAMiSSF50090. SSF50090. 1 hit.
TIGRFAMsiTIGR03888. nitrile_beta. 1 hit.

Sequencei

Sequence statusi: Complete.

P13449-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDGVHDLAGV QGFGKVPHTV NADIGPTFHA EWEHLPYSLM FAGVAELGAF
60 70 80 90 100
SVDEVRYVVE RMEPRHYMMT PYYERYVIGV ATLMVEKGIL TQDELESLAG
110 120 130 140 150
GPFPLSRPSE SEGRPAPVET TTFEVGQRVR VRDEYVPGHI RMPAYCRGRV
160 170 180 190 200
GTISHRTTEK WPFPDAIGHG RNDAGEEPTY HVKFAAEELF GSDTDGGSVV
210
VDLFEGYLEP AA
Length:212
Mass (Da):23,487
Last modified:January 1, 1990 - v1
Checksum:iA0401CA4FC1C2CBE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401M → V in strain: ACV2.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54074 Genomic DNA. Translation: CAA38011.1.
X14668 Genomic DNA. Translation: CAA32798.1.
Z48769 Genomic DNA. Translation: CAA88686.1.
AB016078 Genomic DNA. Translation: BAA36598.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54074 Genomic DNA. Translation: CAA38011.1 .
X14668 Genomic DNA. Translation: CAA32798.1 .
Z48769 Genomic DNA. Translation: CAA88686.1 .
AB016078 Genomic DNA. Translation: BAA36598.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AHJ X-ray 2.65 B/D/F/H 1-212 [» ]
2AHJ X-ray 1.70 B/D 1-212 [» ]
2CYZ X-ray 1.55 B 1-212 [» ]
2CZ0 X-ray 1.50 B 1-212 [» ]
2CZ1 X-ray 1.39 B 1-212 [» ]
2CZ6 X-ray 1.50 B 1-212 [» ]
2CZ7 X-ray 1.80 B 1-212 [» ]
2D0Q X-ray 1.65 B 1-212 [» ]
2QDY X-ray 1.30 B 1-212 [» ]
2ZCF X-ray 1.43 B 1-212 [» ]
2ZPB X-ray 1.30 B 1-212 [» ]
2ZPE X-ray 1.48 B 1-212 [» ]
2ZPF X-ray 1.48 B 1-212 [» ]
2ZPG X-ray 1.39 B 1-212 [» ]
2ZPH X-ray 1.59 B 1-212 [» ]
2ZPI X-ray 1.49 B 1-212 [» ]
3A8G X-ray 1.11 B 1-212 [» ]
3A8H X-ray 1.66 B 1-212 [» ]
3A8L X-ray 1.63 B 1-212 [» ]
3A8M X-ray 1.32 B 1-212 [» ]
3A8O X-ray 1.47 B 1-212 [» ]
ProteinModelPortali P13449.
SMRi P13449. Positions 1-212.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6076N.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P13449.

Miscellaneous databases

EvolutionaryTracei P13449.

Family and domain databases

InterProi IPR024690. CN_hydtase_beta_dom.
IPR008990. Elect_transpt_acc-like_dom.
IPR003168. Nitrile_hydratase_bsu.
[Graphical view ]
Pfami PF02211. NHase_beta. 1 hit.
[Graphical view ]
PIRSFi PIRSF001427. NHase_beta. 1 hit.
SUPFAMi SSF50090. SSF50090. 1 hit.
TIGRFAMsi TIGR03888. nitrile_beta. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Primary structure of nitrile hydratase deduced from the nucleotide sequence of a Rhodococcus species and its expression in Escherichia coli."
    Ikehata O., Nishiyama M., Horinouchi S., Beppu T.
    Eur. J. Biochem. 181:563-570(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: N-774.
  2. "Cloning and characterization of an amidase gene from Rhodococcus species N-774 and its expression in Escherichia coli."
    Hashimoto Y., Nishiyama M., Ikehata O., Horinouchi S., Beppu T.
    Biochim. Biophys. Acta 1088:225-233(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: N-774.
  3. Bigey F., Chebrou H., Arnaud A., Galzy P.
    Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ACV2.
  4. "Functional expression of nitrile hydratase in Escherichia coli: requirement of a nitrile hydratase activator and post-translational modification of a ligand cysteine."
    Nojiri M., Yohda M., Odaka M., Matsushita Y., Tsujimura M., Yoshida T., Dohmae N., Takio K., Endo I.
    J. Biochem. 125:696-704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: N-771.
  5. "Nitrile hydratase of Rhodococcus sp. N-774. Purification and amino acid sequences."
    Endo T., Watanabe I.
    FEBS Lett. 243:61-64(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-19.
    Strain: N-774.
  6. "Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold."
    Huang W., Jia J., Cummings J., Nelson M., Schneider G., Lindqvist Y.
    Structure 5:691-699(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
    Strain: Brevibacterium sp. R312.
  7. "Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms."
    Nagashima S., Nakasako M., Dohmae N., Tsujimura M., Takio K., Odaka M., Yohda M., Kamiya N., Endo I.
    Nat. Struct. Biol. 5:347-351(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiNHAB_RHOER
AccessioniPrimary (citable) accession number: P13449
Secondary accession number(s): Q59789
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 26, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3