Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Putative agmatine deiminase

Gene

aguA

Organism
Shewanella baltica (strain OS185)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Agmatine + H2O = N-carbamoylputrescine + NH3.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei361 – 3611Amidino-cysteine intermediateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciSBAL402882:GJ99-3249-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative agmatine deiminaseUniRule annotation (EC:3.5.3.12UniRule annotation)
Alternative name(s):
Agmatine iminohydrolaseUniRule annotation
Gene namesi
Name:aguAUniRule annotation
Ordered Locus Names:Shew185_3139
OrganismiShewanella baltica (strain OS185)
Taxonomic identifieri402882 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Putative agmatine deiminasePRO_1000070568Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA6WR31.
SMRiA6WR31. Positions 14-369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the agmatine deiminase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000239346.
KOiK10536.
OMAiEVLLAWT.

Family and domain databases

HAMAPiMF_01841. Agmatine_deimin. 1 hit.
InterProiIPR017754. Agmatine_deiminase.
IPR007466. Peptidyl-Arg-deiminase_porph.
[Graphical view]
PfamiPF04371. PAD_porph. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03380. agmatine_aguA. 1 hit.

Sequencei

Sequence statusi: Complete.

A6WR31-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNANVDATP LTTKPSQDGF YMPAEWAAQQ AVWMIWPHRP DNWRSAGAYA
60 70 80 90 100
QATFAKVADA IGGATPVYMG VPKAFLAEAQ KVMPSHVTLV EMDSNDCWAR
110 120 130 140 150
DTGPTVVINA EGECRGVDWG FNAWGGHNGG LYFPWDKDEQ VAQQMLKQHG
160 170 180 190 200
FARYSAPLIL EGGSIHVDGE GTCMTSAECL LNANRNPDLT KEQIEDLLRD
210 220 230 240 250
YLNVKQFIWL QDGVYMDETD GHIDNMCCFA RPGEVILHWT DDEADPQYPR
260 270 280 290 300
SKAALDVLQN TVDAQGRKLK IHLLPQPGPL YCTEEESLGV TEGTGVPRTA
310 320 330 340 350
GERLAGSYVN FLITNHRIVF PLLDPTTDDI AAQKLQEIFP EYEIVGVPAR
360 370
EILLGGGNIH CITQQIPSGK
Length:370
Mass (Da):40,801
Last modified:August 21, 2007 - v1
Checksum:i602238DE2A9FB831
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000753 Genomic DNA. Translation: ABS09270.1.
RefSeqiWP_012089813.1. NC_009665.1.

Genome annotation databases

EnsemblBacteriaiABS09270; ABS09270; Shew185_3139.
KEGGisbm:Shew185_3139.
PATRICi23463263. VBISheBal127872_3388.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000753 Genomic DNA. Translation: ABS09270.1.
RefSeqiWP_012089813.1. NC_009665.1.

3D structure databases

ProteinModelPortaliA6WR31.
SMRiA6WR31. Positions 14-369.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS09270; ABS09270; Shew185_3139.
KEGGisbm:Shew185_3139.
PATRICi23463263. VBISheBal127872_3388.

Phylogenomic databases

HOGENOMiHOG000239346.
KOiK10536.
OMAiEVLLAWT.

Enzyme and pathway databases

BioCyciSBAL402882:GJ99-3249-MONOMER.

Family and domain databases

HAMAPiMF_01841. Agmatine_deimin. 1 hit.
InterProiIPR017754. Agmatine_deiminase.
IPR007466. Peptidyl-Arg-deiminase_porph.
[Graphical view]
PfamiPF04371. PAD_porph. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03380. agmatine_aguA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAGUA_SHEB8
AccessioniPrimary (citable) accession number: A6WR31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: September 7, 2016
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. 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.