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UniProtKB/Swiss-Prot entry P30903

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

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Entry information
Entry name DHAS_NEIMB
Primary accession number P30903
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Aspartate-semialdehyde dehydrogenase
Synonyms ASA dehydrogenase
ASADH
EC 1.2.1.11
Gene name
Name: asd
OrderedLocusNames: NMB2079
From
Neisseria meningitidis serogroup B [TaxID: 491] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae; Neisseria.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MC58 / Serogroup B;
DOI=10.1126/science.287.5459.1809; PubMed=10710307 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.;
"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58.";
Science 287:1809-1815(2000).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-140.
STRAIN=CCUG 37603 / B16B6 / Serogroup B / Serotype 2a;
DOI=10.1016/0378-1119(93)90707-A; PubMed=8101504 [NCBI, ExPASy, EBI, Israel, Japan]
Hatten L., Wang L., Schryvers A.B., Schweizer H.P.;
"Cloning and characterization of the Neisseria meningitidis asd gene.";
Gene 129:123-128(1993).
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
AE002098; AAF42397.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z14063; CAA78444.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E81009; E81009.
RefSeq NP_275068.1; -.
3D structure databases
HSSP P00353; 1BRM. [HSSP ENTRY / PDB]
SMR P30903; 1-369.
ModBase P30903.
Enzyme and pathway databases
BioCyc NMEN122586:NMB_2079-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004073; Molecular function: aspartate-semialdehyde dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0051287; Molecular function: NAD binding (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0019877; Biological process: diaminopimelate biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000319; Asp-semialdehyde_DHase_CS.
IPR011534; Asp_ADH_proteob.
IPR012080; Asp_semialdehyde_DHase.
IPR016040; NAD(P)-bd.
IPR000534; Semialdehyde_DHase_NAD-bd.
IPR012280; Semialdhyde_DHase_C.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF01118; Semialdhyde_dh; 1.
PF02774; Semialdhyde_dhC; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000148; ASA_dh; 1.
TIGRFAMs TIGR01745; asd_gamma; 1.
PROSITE PS01103; ASD; 1.
BLOCKS P30903.
ProtoNet P30903.
Genome annotation databases
GeneID 903977; -.
GenomeReviews AE002098_GR; NMB2079.
KEGG nme:NMB2079; -.
NMPDR fig|122586.1.peg.2002; -.
TIGR NMB2079; -.
Phylogenomic databases
HOGENOM P30903; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Diaminopimelate biosynthesis; Lysine biosynthesis; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   371  371     Aspartate-semialdehyde dehydrogenase. PRO_0000141385
ACT_SITE   135   135        Acyl-thioester intermediate (By similarity). 
CONFLICT   44    44        A -> R (in Ref. 2; CAA78444). 
CONFLICT   117   119        DVL -> NVI (in Ref. 2; CAA78444). 
Sequence information
Length: 371 AA [This is the length of the unprocessed precursor] Molecular weight: 39858 Da [This is the MW of the unprocessed precursor] CRC64: F36BF70BB80075AA [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKVGFVGWRG MVGSVLMQRM KEENDFAHIP EAFFFTTSNV GGAAPDFGQA AKTLLDANNV 

        70         80         90        100        110        120 
AELAKMDIIV TCQGGDYTKS VFQALRDSGW NGYWIDAASS LRMKDDAIIV LDPVNRDVLD 

       130        140        150        160        170        180 
NGLKNGVKNY IGGNCTVSLM LMALGGLFQN DLVEWATSMT YQAASGAGAK NMRELISGMG 

       190        200        210        220        230        240 
AVHAQVADAL ADPAGSILDI DRKVSDFLRS EDYPKANFGV PLAGSLIPWI DVDLGNGQSK 

       250        260        270        280        290        300 
EEWKGGVETN KILGRSDNPT VIDGLCVRVG AMRCHSQAIT LKLKKDLPVS EIETILAGAN 

       310        320        330        340        350        360 
DWVKVIPNEK EASIHELTPA KVTGTLSVPV GRIRKLGMGG EYISAFTVGD QLLWGAAEPL 

       370 
RRVLRIVLGS L
P30903 in FASTA format

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