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Q12572 (LYS2_CANAX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
L-aminoadipate-semialdehyde dehydrogenase large subunit

EC=1.2.1.31
Alternative name(s):
Alpha-aminoadipate reductase
Short name=Alpha-AR
Gene names
Name:LYS2
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length1391 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH.

Catalytic activity

(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.

Cofactor

Binds 1 phosphopantetheine covalently Potential.

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via AAA pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 1/3.

Subunit structure

Heterodimer of an alpha and a beta subunit By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Contains 1 acyl carrier domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13911391L-aminoadipate-semialdehyde dehydrogenase large subunit
PRO_0000193149

Regions

Domain852 – 90251Acyl carrier

Amino acid modifications

Modified residue8841O-(pantetheine 4'-phosphoryl)serine Potential

Sequences

Sequence LengthMass (Da)Tools
Q12572 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: B7E641866235BCDD

FASTA1,391154,741
        10         20         30         40         50         60 
MTDFWLNYLD NPTLSVLPHD FLKPANNKSV EGTYTFNIDN GSTDFKFGLA VFAALVYRLT 

        70         80         90        100        110        120 
GDEDIVIATD ESANTPEFIV RLNLTPELTF QELVSKITKE YENNISQINY KALSEVSHRI 

       130        140        150        160        170        180 
KEAKGLDENP GLFRLSYQHA HSNQQLNTTV EGSIRDLAIY TDGTKFTIYY NALLYSHERV 

       190        200        210        220        230        240 
VICGEQFAQL TTVSGDTDTV IAEVFLITDF HKKNLPDPTI DLDWSGYRGA IQEIFMDNAN 

       250        260        270        280        290        300 
KHPDRTCVVE TVSFLESNSK TRNFSYHKLI KLLIVVGNYL KETGIKKGDI VMIYAYRGVD 

       310        320        330        340        350        360 
LMIAVMGVLK AGATFSVIDP AYPPARQNIY LSVAKPKGLI GLEKAGTLDQ LVVDYISNEL 

       370        380        390        400        410        420 
DVVSTIPQLK VQDDGTLVGG KLEGADNDCL NDYQKFKDQP AGVIVGPDSR PTLSFTSGSE 

       430        440        450        460        470        480 
GIPKGVLGRH YSLAYYFPWM AKRFRLSEKD KFTILSGIAH DPIQRDMFTP LFLGAQLLVP 

       490        500        510        520        530        540 
TADDIGTPGK LADWMAKYGA TVTHLTLAMG QLLSAQATTA IPSLHAFFVG DILTKRDCLR 

       550        560        570        580        590        600 
LQSLAENVFI VNMLWSLSQT QRSVSYFEIK SRKADPTYLK NLKAVMPAGT GMHNVQLLVV 

       610        620        630        640        650        660 
NRNDRSQTCG VGEVGEIYVR AAGLAEGYRG LPDLNAAKFI TNWYVNPDKW IEQDEANKKS 

       670        680        690        700        710        720 
SETSERTWSV KPRDRMYRSG DLGRYFSDGN VECCGRADDQ VKIRGFRIEL GEIDTHLSQH 

       730        740        750        760        770        780 
PLVRENVTLV RRDKNEEPTL ISYIVPKDSP ELKTFFADVD FPLKKSNDPI VKGLVAYREL 

       790        800        810        820        830        840 
IKDIKGYLKK KLASYAIPTI IVPLVKLPLN PNGKVDKPKL PFPDTAQLAA VAKLSVSSHD 

       850        860        870        880        890        900 
AQAAEEENLT KLEEQIRDLW LDVLPNRPAT ISKDDSFFDL GSHSILGTRI FTYEQKLNVE 

       910        920        930        940        950        960 
IPLVSFKGDQ RRPRFPIGLS RYNYSRREQR CRRFLKAKTY TMRRSKELSK ELSKSALLES 

       970        980        990       1000       1010       1020 
YSSLKQLPSG SVNVFVTGAT GFLGSFIVRD LLTARNKNLD IKVYAHVRAS SKEAGLQRLR 

      1030       1040       1050       1060       1070       1080 
QTGITYGIWD ENWAEKIEIV LGDLSKEKFG LDNSQWSDLT NSIDVLFTMV LCHWVYPYSQ 

      1090       1100       1110       1120       1130       1140 
LRMLNVIGTI NVFNMAGEVK LKFFSFVSST SALDTDYFVN LSDELLAQGK NGISEADDLQ 

      1150       1160       1170       1180       1190       1200 
GSAKGLGNGY GQSKWAAEYI IRRAGERGLK GCITRPGYVA GFSKTGASNT DDFLLRMLKG 

      1210       1220       1230       1240       1250       1260 
SAELGLYPDI TNNVNMVPVD HVARVVTATA LNPPSSEELT VAHVTGHPRI LFNNFLGCLK 

      1270       1280       1290       1300       1310       1320 
AYGYEINPAD YPVWTSALEK FVIEESKESA LFPLLHFVLD NLPQDTKAPE LDDSNAAKSL 

      1330       1340       1350       1360       1370       1380 
KQDSKYTGED FSAGKGVDLD QTGVYISYLI KIGFLPKPTG TGEKKLPEVE ISDESLKLIS 

      1390 
GGAGARGSAA K 

« Hide

References

[1]"Molecular analysis of the LYS2 gene of Candida albicans: homology to peptide antibiotic synthetases and the regulation of the alpha-aminoadipate reductase."
Suvarna K., Seah L., Bhattacherjee V., Bhattacharjee J.K.
Curr. Genet. 33:268-275(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 11651 / B792 / 171D.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U58133 Genomic DNA. Translation: AAC02241.1.

3D structure databases

ProteinModelPortalQ12572.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3320.

Enzyme and pathway databases

UniPathwayUPA00033; UER00032.

Family and domain databases

Gene3D1.10.1200.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR010071. AA_adenyl_domain.
IPR009081. Acyl_carrier_prot-like.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR014397. L-NH2adipate-semiAld_DH_lsu.
IPR013120. Male_sterile_NAD-bd.
IPR016040. NAD(P)-bd_dom.
IPR010080. Thioester_reductase-like_dom.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF07993. NAD_binding_4. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
PIRSFPIRSF001617. Alpha-AR. 1 hit.
SUPFAMSSF47336. SSF47336. 1 hit.
TIGRFAMsTIGR01733. AA-adenyl-dom. 1 hit.
TIGR03443. alpha_am_amid. 1 hit.
TIGR01746. Thioester-redct. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYS2_CANAX
AccessionPrimary (citable) accession number: Q12572
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: February 19, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways