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Protein

Omega-amidase NIT2

Gene

Nit2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has a omega-amidase activity. The role of omega-amidase is to remove potentially toxic intermediates by converting alpha-ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively.1 Publication

Catalytic activityi

A monoamide of a dicarboxylate + H2O = a dicarboxylate + NH3.1 Publication

Kineticsi

In solution, alpha-ketoglutaramate is in equilibrium with a cyclic form (2-hydroxy-5-oxoproline), and at pH 8.0 or above, the rate of ring opening is no longer limiting for the omega-amidase reaction.

  1. KM=0.195 mM for alpha-ketoglutaramate at pH=8.51 Publication
  2. KM=1.27 mM for glutaramate at pH=8.51 Publication
  3. KM=0.14 mM for succinamate at pH=8.51 Publication
  4. KM=0.017 mM for alpha-ketosuccinamate at pH=8.51 Publication
  5. KM=0.012 mM for alpha-ketosuccinamate at pH=7.21 Publication
  6. KM=1.48 mM for gamma-monomethyl-alpha-ketoglutarate at pH=7.21 Publication
  7. KM=1.27 mM for glutaramate at pH=7.21 Publication
  8. KM=0.14 mM for glutaramate at pH=7.21 Publication
  1. Vmax=32.0 µmol/min/mg enzyme with alpha-ketoglutaramate as substrate at pH=8.51 Publication
  2. Vmax=1.6 µmol/min/mg enzyme with alpha-ketosuccinamate as substrate at pH=8.51 Publication
  3. Vmax=16 µmol/min/mg enzyme with glutaramate as substrate at pH=8.51 Publication
  4. Vmax=5.1 µmol/min/mg enzyme with glutaramate as substrate at pH=8.51 Publication
  5. Vmax=245.2 µmol/min/mg enzyme with gamma-monomethyl-alpha-ketoglutarate as substrate at pH=7.21 Publication
  6. Vmax=7.5 µmol/min/mg enzyme with glutaramate as substrate at pH=7.21 Publication
  7. Vmax=3.6 µmol/min/mg enzyme with glutaramate as substrate at pH=7.21 Publication
  8. Vmax=2.1 µmol/min/mg enzyme with alpha-ketosuccinamate as substrate at pH=7.21 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei43 – 431Proton acceptorPROSITE-ProRule annotation
Active sitei112 – 1121Proton donorPROSITE-ProRule annotation
Active sitei153 – 1531NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Omega-amidase NIT2 (EC:3.5.1.31 Publication)
Alternative name(s):
Nitrilase homolog 2
Gene namesi
Name:Nit2
Synonyms:D16Ertd502e
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1261838. Nit2.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 276276Omega-amidase NIT2PRO_0000320254Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei68 – 681N6-acetyllysine; alternateCombined sources
Modified residuei68 – 681N6-succinyllysine; alternateCombined sources
Modified residuei123 – 1231N6-succinyllysineCombined sources
Modified residuei130 – 1301N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JHW2.
MaxQBiQ9JHW2.
PaxDbiQ9JHW2.
PRIDEiQ9JHW2.

2D gel databases

REPRODUCTION-2DPAGEIPI00119945.

PTM databases

iPTMnetiQ9JHW2.
PhosphoSiteiQ9JHW2.

Expressioni

Gene expression databases

BgeeiQ9JHW2.
CleanExiMM_NIT2.
GenevisibleiQ9JHW2. MM.

Interactioni

Subunit structurei

May form dimer.1 Publication

Protein-protein interaction databases

IntActiQ9JHW2. 3 interactions.
MINTiMINT-4129730.
STRINGi10090.ENSMUSP00000023432.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi17 – 3317Combined sources
Beta strandi37 – 404Combined sources
Turni43 – 464Combined sources
Turni51 – 533Combined sources
Helixi54 – 574Combined sources
Beta strandi61 – 633Combined sources
Helixi64 – 7613Combined sources
Beta strandi78 – 814Combined sources
Beta strandi85 – 895Combined sources
Beta strandi92 – 1009Combined sources
Beta strandi106 – 1116Combined sources
Beta strandi117 – 1204Combined sources
Turni121 – 1233Combined sources
Beta strandi124 – 1274Combined sources
Helixi128 – 1303Combined sources
Beta strandi140 – 1423Combined sources
Beta strandi147 – 1504Combined sources
Helixi153 – 1575Combined sources
Helixi159 – 1679Combined sources
Beta strandi170 – 1767Combined sources
Helixi183 – 19917Combined sources
Beta strandi202 – 2065Combined sources
Beta strandi214 – 2163Combined sources
Beta strandi223 – 2253Combined sources
Beta strandi231 – 2344Combined sources
Beta strandi237 – 24711Combined sources
Helixi248 – 25710Combined sources
Helixi260 – 2623Combined sources
Turni266 – 2683Combined sources
Beta strandi269 – 2735Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W1VX-ray1.49A/B1-276[»]
ProteinModelPortaliQ9JHW2.
SMRiQ9JHW2. Positions 1-274.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JHW2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 270267CN hydrolasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CN hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0806. Eukaryota.
COG0388. LUCA.
GeneTreeiENSGT00550000074838.
HOGENOMiHOG000222700.
HOVERGENiHBG105126.
InParanoidiQ9JHW2.
KOiK13566.
OMAiNPWGEVI.
OrthoDBiEOG7XDBGD.
PhylomeDBiQ9JHW2.
TreeFamiTF300747.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JHW2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTFRLALIQ LQVSSIKSDN LTRACSLVRE AAKQGANIVS LPECFNSPYG
60 70 80 90 100
TTYFPDYAEK IPGESTQKLS EVAKESSIYL IGGSIPEEDA GKLYNTCSVF
110 120 130 140 150
GPDGSLLVKH RKIHLFDIDV PGKITFQESK TLSPGDSFST FDTPYCKVGL
160 170 180 190 200
GICYDMRFAE LAQIYAQRGC QLLVYPGAFN LTTGPAHWEL LQRARAVDNQ
210 220 230 240 250
VYVATASPAR DDKASYVAWG HSTVVDPWGQ VLTKAGTEET ILYSDIDLKK
260 270
LAEIRQQIPI LKQKRADLYT VESKKP
Length:276
Mass (Da):30,502
Last modified:October 1, 2000 - v1
Checksum:i740FDC44978326D6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF284573 mRNA. Translation: AAF87102.1.
AK003604 mRNA. Translation: BAB22884.1.
AK004535 mRNA. Translation: BAB23354.1.
BC020153 mRNA. Translation: AAH20153.1.
CCDSiCCDS37363.1.
RefSeqiNP_075664.1. NM_023175.1.
UniGeneiMm.383203.

Genome annotation databases

EnsembliENSMUST00000023432; ENSMUSP00000023432; ENSMUSG00000022751.
GeneIDi52633.
KEGGimmu:52633.
UCSCiuc007zna.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF284573 mRNA. Translation: AAF87102.1.
AK003604 mRNA. Translation: BAB22884.1.
AK004535 mRNA. Translation: BAB23354.1.
BC020153 mRNA. Translation: AAH20153.1.
CCDSiCCDS37363.1.
RefSeqiNP_075664.1. NM_023175.1.
UniGeneiMm.383203.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2W1VX-ray1.49A/B1-276[»]
ProteinModelPortaliQ9JHW2.
SMRiQ9JHW2. Positions 1-274.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JHW2. 3 interactions.
MINTiMINT-4129730.
STRINGi10090.ENSMUSP00000023432.

PTM databases

iPTMnetiQ9JHW2.
PhosphoSiteiQ9JHW2.

2D gel databases

REPRODUCTION-2DPAGEIPI00119945.

Proteomic databases

EPDiQ9JHW2.
MaxQBiQ9JHW2.
PaxDbiQ9JHW2.
PRIDEiQ9JHW2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023432; ENSMUSP00000023432; ENSMUSG00000022751.
GeneIDi52633.
KEGGimmu:52633.
UCSCiuc007zna.1. mouse.

Organism-specific databases

CTDi56954.
MGIiMGI:1261838. Nit2.

Phylogenomic databases

eggNOGiKOG0806. Eukaryota.
COG0388. LUCA.
GeneTreeiENSGT00550000074838.
HOGENOMiHOG000222700.
HOVERGENiHBG105126.
InParanoidiQ9JHW2.
KOiK13566.
OMAiNPWGEVI.
OrthoDBiEOG7XDBGD.
PhylomeDBiQ9JHW2.
TreeFamiTF300747.

Miscellaneous databases

EvolutionaryTraceiQ9JHW2.
NextBioi309239.
PROiQ9JHW2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHW2.
CleanExiMM_NIT2.
GenevisibleiQ9JHW2. MM.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Crystal structure of the worm NitFhit Rosetta stone protein reveals a Nit tetramer binding two Fhit dimers."
    Pace H.C., Hodawadekar S.C., Draganescu A., Huang J., Bieganowski P., Pekarsky Y., Croce C.M., Brenner C.
    Curr. Biol. 10:907-917(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Mammary tumor.
  4. "Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2."
    Jaisson S., Veiga-da-Cunha M., Van Schaftingen E.
    Biochimie 91:1066-1071(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  5. "Identification of the putative tumor suppressor Nit2 as omega-amidase, an enzyme metabolically linked to glutamine and asparagine transamination."
    Krasnikov B.F., Chien C.-H., Nostramo R., Pinto J.T., Nieves E., Callaway M., Sun J., Huebner K., Cooper A.J.L.
    Biochimie 91:1072-1080(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-123 AND LYS-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  8. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Functional proteomic and structural insights into molecular recognition in the nitrilase family enzymes."
    Barglow K.T., Saikatendu K.S., Bracey M.H., Huey R., Morris G.M., Olson A.J., Stevens R.C., Cravatt B.F.
    Biochemistry 47:13514-13523(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS).

Entry informationi

Entry nameiNIT2_MOUSE
AccessioniPrimary (citable) accession number: Q9JHW2
Secondary accession number(s): Q9CTG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2000
Last modified: March 16, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.