NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ng1447; PubMed=15467720 [NCBI, ExPASy, EBI, Israel, Japan]
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.;
"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity.";
Nat. Genet. 36:1165-1173(2004).

Comments

FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2) (By similarity).
CATALYTIC ACTIVITY: N²-succinyl-L-arginine + 2 H₂O = N²-succinyl-L-ornithine + 2 NH₃ + CO₂.
PATHWAY: Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 2/5 .
SUBUNIT: Homodimer (By similarity).
SIMILARITY: Belongs to the succinylarginine dihydrolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CR628337; CAH15907.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_127006.1; -.

3D structure databases

ModBase

Q5WVZ3.

Enzyme and pathway databases

BioCyc

LPNE297245:LPL1667-MON; -.

Organism-specific databases

LegioList

lpl1667; -.

Ontologies

GO:0009015;	Molecular function: N-succinylarginine dihydrolase activity (inferred from electronic annotation from HAMAP).
GO:0019544;	Biological process: arginine catabolic process to glutamate (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01172; -; 1.
PBIL [Tree]

InterPro

IPR007079; SuccinylArg_d-OHase_AstB.
Graphical view of domain structure.

Gene3D

G3DSA:3.75.10.20; SuccinylArg_di_hydro; 1.

Pfam

PF04996; AstB; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR03241; arg_catab_astB; 1.

Genome annotation databases

GeneID

3113610; -.

GenomeReviews

CR628337_GR; lpl1667.

KEGG

lpf:lpl1667; -.

NMPDR

fig|297245.3.peg.1849; -.

Phylogenomic databases

HOGENOM

Q5WVZ3; -.

Genome annotation databases

CMR

Q5WVZ3; lpl1667.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Arginine metabolism; Complete proteome; Hydrolase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 448`	`448`	`N-succinylarginine dihydrolase.`	`PRO_0000262355`
`REGION`	`19 28`	`10`	`Substrate binding (By similarity).`
`REGION`	`137 138`	`2`	`Substrate binding (By similarity).`
`ACT_SITE`	`174 174`		`By similarity.`
`ACT_SITE`	`252 252`		`By similarity.`
`ACT_SITE`	`372 372`		`Nucleophile (By similarity).`
`BINDING`	`110 110`		`Substrate (By similarity).`
`BINDING`	`216 216`		`Substrate (By similarity).`
`BINDING`	`254 254`		`Substrate (By similarity).`
`BINDING`	`366 366`		`Substrate (By similarity).`

Sequence information

Length: 448 AA [This is the length of the unprocessed precursor]

Molecular weight: 50198 Da [This is the MW of the unprocessed precursor]

CRC64: 86B2FBD856161173 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNVYELNMDG LVGQTHHYAG LSSGNIASTN NALSISNPQA AARQGLEKMR RLYNMGLKQG 

        70         80         90        100        110        120 
LLPPHQRPNL NLLYQLGFKG TPSEQINKAY KTAPELLSAC YSASCMWTAN AATVSASVDT 

       130        140        150        160        170        180 
EDNKVHFTAA NLISNLHRHQ EADFSKKLLE FIFSNSDYFN HHPLLPKSMG TSDEGAANHN 

       190        200        210        220        230        240 
RLCQSHAHSG INLFVYGKKV LGNHQFEQSP IKYPARQTKE ASEAIARNHL LNPERVIFAC 

       250        260        270        280        290        300 
QNPLAIDQGV FHNDVISVAN EHVFLVHEEA FYNQTYVLDQ LREKADFPLV IIQISKEQIS 

       310        320        330        340        350        360 
VSEAVDTYLF NSQLITLPDQ KNMILIAPAE CQANLKVKTC IDGLVADPQN PINSVYYLDL 

       370        380        390        400        410        420 
KQSMRNGGGP ACLRLRVPLN DYELKAMHQG ILIDNDLLDI LDKWVLKYYR TELKISDLAD 

       430        440 
PQLLYECLDA LDELTQILKL GSIYPFQS

Q5WVZ3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools