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Protein
Submitted name:

Amidohydrolase 2

Gene

Saro_0799

Organism
Novosphingobium aromaticivorans (strain DSM 12444 / F199)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi19 – 191CalciumCombined sources
Metal bindingi19 – 191ManganeseCombined sources
Metal bindingi188 – 1881Calcium; via tele nitrogenCombined sources
Metal bindingi188 – 1881Manganese; via tele nitrogenCombined sources
Metal bindingi314 – 3141CalciumCombined sources
Metal bindingi314 – 3141ManganeseCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

Keywords - Ligandi

CalciumCombined sources, ManganeseCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BioCyciNARO279238:GHBU-809-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
Amidohydrolase 2Imported
Gene namesi
Ordered Locus Names:Saro_0799Imported
OrganismiNovosphingobium aromaticivorans (strain DSM 12444 / F199)Imported
Taxonomic identifieri279238 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium
ProteomesiUP000009134 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi279238.Saro_0799.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4INFX-ray1.48A/B/C/D1-351[»]
4QRNX-ray1.07A/B/C/D1-351[»]
4QS5X-ray1.80A/B/C/D1-351[»]
4QS6X-ray1.76A/B1-351[»]
4QTGX-ray1.47A/B1-351[»]
ProteinModelPortaliQ2GA79.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2159.
HOGENOMiHOG000254104.
KOiK14333.
OMAiDQHGIDM.
OrthoDBiEOG628F7F.

Family and domain databases

InterProiIPR006992. Amidohydro_2.
[Graphical view]
PfamiPF04909. Amidohydro_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2GA79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQDLKTGGE QGYLRIATEE AFATREIIDV YLRMIRDGTA DKGMVSLWGF
60 70 80 90 100
YAQSPSERAT QILERLLDLG ERRIADMDAT GIDKAILALT SPGVQPLHDL
110 120 130 140 150
DEARTLATRA NDTLADACQK YPDRFIGMGT VAPQDPEWSA REIHRGAREL
160 170 180 190 200
GFKGIQINSH TQGRYLDEEF FDPIFRALVE VDQPLYIHPA TSPDSMIDPM
210 220 230 240 250
LEAGLDGAIF GFGVETGMHL LRLITIGIFD KYPSLQIMVG HMGEALPYWL
260 270 280 290 300
YRLDYMHQAG VRSQRYERMK PLKKTIEGYL KSNVLVTNSG VAWEPAIKFC
310 320 330 340 350
QQVMGEDRVM YAMDYPYQYV ADEVRAMDAM DMSAQTKKKF FQTNAEKWFK

L
Length:351
Mass (Da):39,852
Last modified:March 21, 2006 - v1
Checksum:iF60CF52989252B7F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000248 Genomic DNA. Translation: ABD25244.1.
RefSeqiWP_011444458.1. NC_007794.1.
YP_496078.1. NC_007794.1.

Genome annotation databases

EnsemblBacteriaiABD25244; ABD25244; Saro_0799.
KEGGinar:Saro_0799.
PATRICi22784222. VBINovAro50627_0819.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000248 Genomic DNA. Translation: ABD25244.1.
RefSeqiWP_011444458.1. NC_007794.1.
YP_496078.1. NC_007794.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4INFX-ray1.48A/B/C/D1-351[»]
4QRNX-ray1.07A/B/C/D1-351[»]
4QS5X-ray1.80A/B/C/D1-351[»]
4QS6X-ray1.76A/B1-351[»]
4QTGX-ray1.47A/B1-351[»]
ProteinModelPortaliQ2GA79.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279238.Saro_0799.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD25244; ABD25244; Saro_0799.
KEGGinar:Saro_0799.
PATRICi22784222. VBINovAro50627_0819.

Phylogenomic databases

eggNOGiCOG2159.
HOGENOMiHOG000254104.
KOiK14333.
OMAiDQHGIDM.
OrthoDBiEOG628F7F.

Enzyme and pathway databases

BioCyciNARO279238:GHBU-809-MONOMER.

Family and domain databases

InterProiIPR006992. Amidohydro_2.
[Graphical view]
PfamiPF04909. Amidohydro_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 12444 / F199Imported.
  2. "Crystal structure of amidohydrolase sarp_0799 (target efi-505250) from novosphingobium aromaticivorans."
    Patskovsky Y., Toro R., Bhosle R., Hillerich B., Seidel R.D., Washington E., Scott Glenn A., Chowdhury S., Evans B., Hammonds J., Zencheck W.D., Imker H.J., Gerlt J.A., Raushel F.M., Almo S.C.
    Submitted (JAN-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH CALCIUM.
  3. "Crystal Structure of 5-CARBOXYVANILLATE Decarboxylase from Novosphingobium Aromaticivorans."
    Patskovsky Y., Vladimirova A., Toro R., Bhosle R., Gerlt J.A., Raushel F.M., Almo S.C.
    Submitted (JUL-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
  4. "Crystal Structure of 5-Carboxyvanillate Decarboxylase from Novosphingobium Aromaticivorans."
    Patskovsky Y., Vladimirova A., Toro R., Bhosle R., Raushel F.M., Almo S.C.
    Submitted (JUL-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.07 ANGSTROMS) IN COMPLEX WITH MANGANESE.
  5. "Crystal Structure of 5-Carboxyvanillate Decarboxylase LIGW2 from Novosphingobium Aromaticivorans."
    Patskovsky Y., Vladimirova A., Toro R., Bhosle R., Raushel F.M., Almo S.C.
    Submitted (JUL-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) IN COMPLEX WITH MANGANESE.
  6. "Crystal Structure of Ligw2 Decarboxylase from Novosphingobium Aromaticivorans."
    Patskovsky Y., Vladimirova A., Toro R., Bhosle R., Raushel F.M., Almo S.C.
    Submitted (JUL-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS).

Entry informationi

Entry nameiQ2GA79_NOVAD
AccessioniPrimary (citable) accession number: Q2GA79
Entry historyi
Integrated into UniProtKB/TrEMBL: March 21, 2006
Last sequence update: March 21, 2006
Last modified: May 27, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.