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UniProtKB/Swiss-Prot entry Q8A1A7

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ARGC_BACTN
Primary accession number Q8A1A7
Secondary accession numbers None
Integrated into Swiss-Prot on February 2, 2004
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 47)
Name and origin of the protein
Protein name N-acetyl-gamma-glutamyl-phosphate reductase
Synonyms AGPR
EC 1.2.1.38
N-acetyl-glutamate semialdehyde dehydrogenase
NAGSA dehydrogenase
Gene name
Name: argC
OrderedLocusNames: BT_3759
From
Bacteroides thetaiotaomicron [TaxID: 818] [HAMAP proteome]
Taxonomy Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
DOI=10.1126/science.1080029; PubMed=12663928 [NCBI, ExPASy, EBI, Israel, Japan]
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.;
"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
Science 299:2074-2076(2003).
Comments
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
AE015928; AAO78864.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_812670.1; -.
3D structure databases
ModBase Q8A1A7.
Enzyme and pathway databases
BioCyc BTHE226186:BT_3759-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003942; Molecular function: N-acetyl-gamma-glutamyl-phosphate reductase activity (inferred from electronic annotation from HAMAP).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0006526; Biological process: arginine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
HAMAP MF_00150; -; 1.
PBIL [Tree]
InterPro IPR000706; AGPR_act_site.
IPR000534; Semialdehyde_DHase_NAD-bd.
IPR012280; Semialdhyde_DHase_C.
Graphical view of domain structure.
Pfam PF01118; Semialdhyde_dh; 1.
PF02774; Semialdhyde_dhC; 1.
Pfam graphical view of domain structure.
ProDom PD003765; AGPR_act_site; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01850; argC; 1.
PROSITE PS01224; ARGC; 1.
BLOCKS Q8A1A7.
ProtoNet Q8A1A7.
Genome annotation databases
GeneID 1076380; -.
GenomeReviews AE015928_GR; BT_3759.
KEGG bth:BT_3759; -.
NMPDR fig|226186.1.peg.3757; -.
Phylogenomic databases
HOGENOM Q8A1A7; -.
Genome annotation databases
CMR Q8A1A7; BT_3759.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; Cytoplasm; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   322  322     N-acetyl-gamma-glutamyl-phosphate reductase. PRO_0000112386
ACT_SITE   132   132        By similarity. 
Sequence information
Length: 322 AA [This is the length of the unprocessed precursor] Molecular weight: 35838 Da [This is the MW of the unprocessed precursor] CRC64: 074D784C4F7AB7F7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MIKAGIIGGA GYTAGELIRL LLNHPETEIV FINSSSNAGN RITDVHEGLY GETDLRFTDQ 

        70         80         90        100        110        120 
LPLDAIDVLF FCTAHGDTKK FMESHNVPED LKIIDLSMDY RIKSDDHDFI YGLPELNRRA 

       130        140        150        160        170        180 
TCTAKHVANP GCFATCIQLG LLPLAKNLML TGDVSVNAIT GSTGAGVKPG ATSHFSWRNN 

       190        200        210        220        230        240 
NISIYKAFDH QHVPEIKQSL KQLQNSFDSE IDFIPYRGDF PRGIFATLVV KTKVALEEIV 

       250        260        270        280        290        300 
RMYEEYYAKD SFVHIVDKNI DLKQVVNTNK CLIHLEKHGD KLLIISCIDN LLKGASGQAV 

       310        320 
HNMNLMFNLE ETVGLRLKPS AF
Q8A1A7 in FASTA format

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