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UniProtKB/Swiss-Prot entry P40976


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

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Entry information
Entry name LYS2_SCHPO
Primary accession number P40976
Secondary accession number Q9P770
Integrated into Swiss-Prot on February 1, 1995
Sequence was last modified on February 21, 2001 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 75)
Name and origin of the protein
Protein name L-aminoadipate-semialdehyde dehydrogenase
Synonyms EC 1.2.1.31
Alpha-aminoadipate reductase
Alpha-AR
Gene name
Name: lys1
ORFNames: SPAP7G5.04c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1007/BF00315779; PubMed=8590464 [NCBI, ExPASy, EBI, Israel, Japan]
Ford R.A., Bhattacharjee J.K.;
"Molecular properties of the lys1+ gene and the regulation of alpha-aminoadipate reductase in Schizosaccharomyces pombe.";
Curr. Genet. 28:131-137(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
MUTAGENESIS OF GLY-913 AND SER-916.
STRAIN=ATCC 38366 / 972;
DOI=10.1002/yea.1179; PubMed=15546125 [NCBI, ExPASy, EBI, Israel, Japan]
Guo S., Bhattacharjee J.K.;
"Posttranslational activation, site-directed mutation and phylogenetic analyses of the lysine biosynthesis enzymes alpha-aminoadipate reductase Lys1p (AAR) and the phosphopantetheinyl transferase Lys7p (PPTase) from Schizosaccharomyces pombe.";
Yeast 21:1279-1288(2004).
[4]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
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
U15923; AAC15909.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329670; CAB88271.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S57264; S57264.
RefSeq NP_594314.1; -.
3D structure databases
HSSP P14687; 1AMU. [HSSP ENTRY / PDB]
ModBase P40976.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-001916-MON; -.
Organism-specific databases
GeneDB_Spombe SPAP7G5.04c; -.
Gene expression databases
ArrayExpress P40976; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0000036; Molecular function: acyl carrier activity (inferred from electronic annotation from InterPro).
GO:0000062; Molecular function: acyl-CoA binding (inferred from direct assay from GeneDB_SPombe).
GO:0004043; Molecular function: L-aminoadipate-semialdehyde dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0016874; Molecular function: ligase activity (inferred from electronic annotation from InterPro).
GO:0031177; Molecular function: phosphopantetheine binding (inferred from electronic annotation from InterPro).
GO:0009085; Biological process: lysine 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 IPR010071; AA_adenyl_dom.
IPR009081; ACP_like.
IPR000873; AMP-dep_Synth/Lig.
IPR014397; L-NH2adipate-semiAld_DH_lsu.
IPR013120; Male_sterile_NAD-bd.
IPR016040; NAD(P)-bd.
IPR006163; Phsphopanteth_bd.
IPR006162; Ppantne_S.
IPR010080; Thioester_reductase.
Graphical view of domain structure.
Gene3D G3DSA:1.10.1200.10; ACP_like; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF00501; AMP-binding; 1.
PF07993; NAD_binding_4; 1.
PF00550; PP-binding; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001617; Alpha-AR; 1.
PRINTS PR00154; AMPBINDING.
TIGRFAMs TIGR01733; AA-adenyl-dom; 1.
TIGR03443; alpha_am_amid; 1.
TIGR01746; Thioester-redct; 1.
PROSITE PS50075; ACP_DOMAIN; 1.
PS00455; AMP_BINDING; 1.
PS00012; PHOSPHOPANTETHEINE; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P40976.
Genome annotation databases
GeneID 2542079; -.
KEGG spo:SPAP7G5.04c; -.
NMPDR fig|4896.1.peg.4284; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amino-acid biosynthesis; Complete proteome; Cytoplasm; Lysine biosynthesis; NADP; Oxidoreductase; Phosphopantetheine.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1419  1419     L-aminoadipate-semialdehyde dehydrogenase. PRO_0000193152
DOMAIN   885    953  69     Acyl carrier. 
BINDING   916    916        Phosphopantetheine (covalent) (Potential). 
MUTAGEN   913    913        G->A: No activity. 
MUTAGEN   916    916        S->A,T: No activity. 
CONFLICT   90     91        MT -> IA (in Ref. 1; AAC15909). 
CONFLICT   196    196        Missing (in Ref. 1; AAC15909). 
CONFLICT   487    487        D -> DG (in Ref. 1; AAC15909). 
CONFLICT   500    500        R -> G (in Ref. 1; AAC15909). 
CONFLICT   600    602        Missing (in Ref. 1). 
CONFLICT   620    621        AR -> GP (in Ref. 1; AAC15909). 
CONFLICT   712    712        Y -> S (in Ref. 1; AAC15909). 
CONFLICT   926    928        LRK -> PSQ (in Ref. 1; AAC15909). 
CONFLICT   1203   1205        VVV -> AAA (in Ref. 1; AAC15909). 
CONFLICT   1225   1228        LVRM -> WSK (in Ref. 1; AAC15909). 
CONFLICT   1239   1239        P -> A (in Ref. 1; AAC15909). 
Sequence information
Length: 1419 AA [This is the length of the unprocessed precursor] Molecular weight: 156894 Da [This is the MW of the unprocessed precursor] CRC64: 09AFBEFE09F21A0C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSQTAPSDTE YNQRLERWSE RLKSQTISHL PTDYSRPVPS RLVEAVFERT LPEDAKTALI 

        70         80         90        100        110        120 
KVYVAAQAKG ILVTPFNILL TIFIILVSRM TGDEDISIGT SSENAIPFVL RTFIQPSDSF 

       130        140        150        160        170        180 
LDLLAKVCDL EKEGSSDAVD FSDLINFLNA KLSKKDDPRK TLVHLRFYNA PDAPSENFLS 

       190        200        210        220        230        240 
TTGLDVDLTV LVSVKKPSDQ LTSLRSQFTF PDLQLKLIYN QLLFSESRVN IVADQLLKLV 

       250        260        270        280        290        300 
VSASKDVTGP IGALDLMTPT QMNVLPDPTV DLDWSGYRGA IQDIFASNAA KFPDRECIVV 

       310        320        330        340        350        360 
TPSVTIDAPV TSYTYRQIDE SSNILAHHLV KNGIERGDVV MVYAYRGVDL VVAVMGVLKA 

       370        380        390        400        410        420 
GATFSVIDPA YPPARQIIYL SVAKPRALVV LEDAGVLSPT VVEYVEKSLE LKTYVPALKL 

       430        440        450        460        470        480 
AKDGSLTGGS VSKGADDILQ HVLHLKSEQT GVVVGPDSTP TLSFTSGSEG IPKGVKGRHF 

       490        500        510        520        530        540 
SLAYYFDWMA QEFNLSESDR FTMLSGIAHD PIQRDIFTPL FLGASLIVPT AEDIGTPGQL 

       550        560        570        580        590        600 
AQWANKYKVT VTHLTPAMGQ LLAAQADEPI PSLHHAFFVG DILTKRDCLR LQVLANNVNV 

       610        620        630        640        650        660 
VNMYGTTETQ RSVSYFVVPA RSQDQTFLES QKDVIPAGRG MKNVQLLVIN RFDTNKICGI 

       670        680        690        700        710        720 
GEVGEIYLRA GGLAEGYLGN DELTSKKFLK SWFADPSKFV DRTPENAPWK PYWFGIRDRM 

       730        740        750        760        770        780 
YRSGDLGRYL PTGNVECSGR ADDQIKIRGF RIELGEINTH LSRHPNVREN ITLVRRDKDE 

       790        800        810        820        830        840 
EPTLVAYIVP QGLNKDDFDS ATESEDIVVN GLKKYRKLIH DIREYLKTKL PSYAIPSVIV 

       850        860        870        880        890        900 
PLHKMPLNPN GKIDKPALPF PDTSQLAAAS RSHSKHGVDE TLTATERDIR DIWLRIIPHA 

       910        920        930        940        950        960 
TDVNKKASFF DIGGHSILAT RLIFELRKKF AVNVPLGLVF SEPTIEGLAK EIERMKSGEM 

       970        980        990       1000       1010       1020 
ISVMDIGKEE TREPEIEYGK DALDLVDLIP KEFPTSKDLG IDEPKTVFLT GANGYLGVFI 

      1030       1040       1050       1060       1070       1080 
LRDLMTRSSN LKVIALVRAS SEEHGLKRLK DSCTAYGVWD ESWAQKISVV NGDLALENWG 

      1090       1100       1110       1120       1130       1140 
IEERKWNKLT EVVDYVIHNG ALVHWVYPYS KLRGPNVMGT ITALKLCSLG KGKSLSFVSS 

      1150       1160       1170       1180       1190       1200 
TSTVDTEYYV NLSNEITSKG GNGIPESDPL QGSSKDLHTG YGQSKWVSEY LVRQAGLRGL 

      1210       1220       1230       1240       1250       1260 
RGVVVRPGYI LGDSKSGAIN TDDFLVRMVK GCIELGLYPN INNTVNMVPA DHVARVVTAS 

      1270       1280       1290       1300       1310       1320 
AFHPEQGVIV AHVTSHPRLR FNQFLGTLST FGFNTKLSEY VNWRIALERF VINESHDSAL 

      1330       1340       1350       1360       1370       1380 
YPLLHFVLDN LPANTKAPEL DDTNTREILK RDASWTNVDV SNGAAILEHE MGLYLSYLVA 

      1390       1400       1410 
IGFLPKPTLE GKKLPEVKIN EATLEKLASA GGRGGAPTH 

P40976 in FASTA format

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