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Q75BB3 (LYS2_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:ADL346W
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeEremothecium

Protein attributes

Sequence length1385 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 By similarity.

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 – 13851385L-aminoadipate-semialdehyde dehydrogenase large subunit
PRO_0000193148

Regions

Domain848 – 91770Acyl carrier

Amino acid modifications

Modified residue8801O-(pantetheine 4'-phosphoryl)serine Potential

Sequences

Sequence LengthMass (Da)Tools
Q75BB3 [UniParc].

Last modified January 9, 2013. Version 2.
Checksum: DE96D1018986F338

FASTA1,385151,953
        10         20         30         40         50         60 
MCAVLEPSMI RWLSEVDNIV VSSLPSDYIP SGPAGVKAES CEVELPGSFG VIDEEDSYIR 

        70         80         90        100        110        120 
LLSAFATLVC RMSGESDVAM YSKANRLLKL AVPPGVAFQQ LRASVTEAVE GTLALPAVDF 

       130        140        150        160        170        180 
DELSALEREK KQLDYYPQYF KVGVVTAADK TKLDQFRYHK FELLLRQVTS SRFEMVYDSE 

       190        200        210        220        230        240 
RFSPDRIGEL GEQLVQFLTL VEAKDDADVY AISLVTSGAS RVLPDPTTDL GWGQFRGAIH 

       250        260        270        280        290        300 
DIFQHHAETR PDRLCVVETG VGQVAARTFT YSAINCASNI VAHYLLARGI RRGDVVMIYS 

       310        320        330        340        350        360 
TRGVDLLVSV LGVLKSGAVF SVIDPAYPPA RQNVYLGVAK PAGLIVIQAA GQLDEAVEAF 

       370        380        390        400        410        420 
IRDNLSLKAR LPALALQTDG AILGGTLPDF HLDTLVPFAS LKNTRTDVVV GPDSNPTLSF 

       430        440        450        460        470        480 
TSGSEGIPKG VLGRHFSLTY YFDWMAKRFG LSEDDKFTML SGIAHDPIQR DMFTPIYLGA 

       490        500        510        520        530        540 
QLLVPQEDDI GTPGRLATWM ATHGATVTHL TPAMGQVLTA DATTPFPSLK RAFFVGDVLT 

       550        560        570        580        590        600 
KRDCARLQSL AENVAIVNMY GSTETQRAVS YFEVPSCSSN PSYLDNLKSI IPAGRGMHNV 

       610        620        630        640        650        660 
QLLIVNRHDR TKLCGIGEVG EIYVRAGGLS EGYRGLPEIN KEKFIDNWFV DAGHWGGLDL 

       670        680        690        700        710        720 
SGDEPWRNYW LGVRDRLYRT GDLGRYLPNG DCECCGRADD QVKIRGFRIE LGEIDTNISQ 

       730        740        750        760        770        780 
YPLCRENITL LRKDQNGEST LISYLVPRSD QKALASFISA VPESIATESI AGSLIKYHKL 

       790        800        810        820        830        840 
INDIRGFLKK RLAGYAIPTL IMVMERLPLN PNGKIDKNKL QFPEPTELDR ASEHFASETL 

       850        860        870        880        890        900 
GLSSFSPLEQ EIRKIWLDLL PTRPAITSSD ESFFDLGGTS ILATRMAIVL RNRLNISLAL 

       910        920        930        940        950        960 
STIFRYPTVK ELAKEISRVR GTISDDKSSN SGTTEYYADA KHVSEAELAS KYESRLSLLP 

       970        980        990       1000       1010       1020 
SGATSAPVYV FLTGVTGFLG CHILADLLNR SRKPYDITVY AHVRASDESS ALQRIKSVCT 

      1030       1040       1050       1060       1070       1080 
AYGLWKNAYA PRIKVVLGNL AEKQFGLPKK AWHDLQEGID VIIHNAALVH WVYPYSKLRE 

      1090       1100       1110       1120       1130       1140 
ANVLSTVNVL NLAAAGKAKY FTFVSSTSAL DTKHYLELSN AAIESGGSGV PEDDDLMGGS 

      1150       1160       1170       1180       1190       1200 
LGLKGGYGQS KWAAEFIIKR AGERGLRGCI LRPGYVTGSP STGASNADDF LLRFLRGCVQ 

      1210       1220       1230       1240       1250       1260 
LGKIPDIEGT VNMVPVDYVA RLATAASFSS SGNTHMMVVN VNAKPRISFR DYLLALKEYG 

      1270       1280       1290       1300       1310       1320 
YQVTSVPYDE WSKALESSSD EENPLYPLLY LVLDDLPKKL RSPELDTTNA KFVLEEDFAR 

      1330       1340       1350       1360       1370       1380 
TNIEPIIITS VSLEVVGSYI SFLHKLGFLE EPAKGSRPLP NISLSDEQIS LIAAVATARS 


STAKP 

« Hide

References

« Hide 'large scale' references
[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.
[2]"Genomes of Ashbya fungi isolated from insects reveal four mating-type loci, numerous translocations, lack of transposons, and distinct gene duplications."
Dietrich F.S., Voegeli S., Kuo S., Philippsen P.
G3 (Bethesda) 3:1225-1239(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 543-570; 575; 578; 587 AND 591.
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016817 Genomic DNA. Translation: AAS51573.2.
RefSeqNP_983749.2. NM_209102.2.

3D structure databases

ProteinModelPortalQ75BB3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33169.AGOS_ADL346W.

Proteomic databases

PRIDEQ75BB3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4619884.
KEGGago:AGOS_ADL346W.

Phylogenomic databases

eggNOGCOG3320.
HOGENOMHOG000191209.
KOK00143.
OrthoDBEOG74TX6Z.

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.
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.
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_ASHGO
AccessionPrimary (citable) accession number: Q75BB3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 9, 2013
Last modified: February 19, 2014
This is version 75 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