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Q6FMI5 (LYS2_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 71. 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:CAGL0K07788g
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Nakaseomyces › mitosporic Nakaseomyces ›

Protein attributes

Sequence length1374 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 – 13741374L-aminoadipate-semialdehyde dehydrogenase large subunit
PRO_0000193150

Regions

Domain833 – 90270Acyl carrier

Amino acid modifications

Modified residue8651O-(pantetheine 4'-phosphoryl)serine Potential

Sequences

Sequence LengthMass (Da)Tools
Q6FMI5 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: FF8BF53926B4B184

FASTA1,374152,537
        10         20         30         40         50         60 
MSWKERLDNP TLSVWPHDYL RPHAEPFVEQ GTYSISIPQL SGDYATLLAA WTALLYRVTG 

        70         80         90        100        110        120 
DDDIVLYVRD NKVLRFTITP ELTFTQLQNK INEQLAELAN VEGTNFDALS ESLQKESGLE 

       130        140        150        160        170        180 
RPPQLFRIAC VTEDLQLDRY THSPLDIGLQ LHESSSDVSI VFNKLLFSQD RITILADQLT 

       190        200        210        220        230        240 
LFLTSVLQNA KQVFTKVSLI TDSSTSILPD PKANLDWCGF VGCIHDIFQD NAEKFPERTC 

       250        260        270        280        290        300 
VVETPPINST KTRTFTYKDI NEASNIVAHY LINTGIKRGD VVMIYSSRGV DLMVCVMGVL 

       310        320        330        340        350        360 
KAGATFSVID PAYPPARQTI YLGVAKPKGL IVIRAAGQLD QLVEDYITKE LDLVSRIPSI 

       370        380        390        400        410        420 
AIQDNGTVEG GSLPSESGDV LASYTELKST RTGVVVGPDS NPTLSFTSGS EGIPKGVLGR 

       430        440        450        460        470        480 
HFSLAYYFSW MAKQFNLSEN DKFTMLSGIA HDPIQRDMFT PLFLGAQLYV PTQDDIGTPG 

       490        500        510        520        530        540 
RLAEWMGKYG CTVTHLTPAM GQLLTAQAVT PFPKLHHAFF VGDILTKRDC LRLQTLAENC 

       550        560        570        580        590        600 
CIVNMYGTTE TQRAVSYFEV TSRSQDPHFL KKLKDVMPAG RGMKNVQLLV VNRNDRTQVC 

       610        620        630        640        650        660 
GVGEIGEIYV RAGGLAEGYR GLPDLNKEKF VNNWFVEEGH WNYLDKDLEA PWKEFWQGPR 

       670        680        690        700        710        720 
DRLYRTGDLG RYLPNGDCEC CGRADDQVKI RGFRIELGEI DTNISQHPLV RENITLVRNN 

       730        740        750        760        770        780 
LEGEKCLVTY MVPRFDKPEL ENFKIEVPSN ISDDPVVCGL IGYSPFTKDL KAFLKKRLAS 

       790        800        810        820        830        840 
YAIPSLIIVL PKLPLNPNGK VDKPKLQFPT VKQLELVAKN SSIDINDSEF NQQEREIRDL 

       850        860        870        880        890        900 
WLECLPTKPT SISPEDSFFD LGGHSILATK MIFTVKKQLN VELPLGTIFK YPTIKAFAAE 

       910        920        930        940        950        960 
VSRLKSTDKI EEETTALTAD YASDAASLID TLPKSYPAAR ALGSPSEMAG PTTVNIFVTG 

       970        980        990       1000       1010       1020 
VTGFLGSFIL SDILNRTVTG VNFKIFAHVR AADETSGLDR IRKAGTVYGT WKEEYANSLQ 

      1030       1040       1050       1060       1070       1080 
VVIGDLSKKN FGLTDDKWSH LSETIDIIIH NGALVHWVYP YSKLRNANVV STINIMNLAS 

      1090       1100       1110       1120       1130       1140 
EGKPKLFNFV SSTSVLDTNH YFELSDKLQQ SGKEGIPESD DLMGSSLGLT SGYGQSKWAA 

      1150       1160       1170       1180       1190       1200 
EHIIRAAGKR GLRGSIIRPG YVTGASYNGS SNTDDFLLRF LKSAVQLGKI PDINNTVNMV 

      1210       1220       1230       1240       1250       1260 
PVDQVARVVV AASINPPCGD DLCVVHVNAH PRIIFKDYLY ELKNYGYDVE IENYEQWKKT 

      1270       1280       1290       1300       1310       1320 
LEEAVIERSE DNALFPLLHM VLGDLEDSTK APELDDKNAI TSLRADIEWT NEDRTKGMGA 

      1330       1340       1350       1360       1370 
TPEQIGIYIS FLESVGFLPH PKHFGDKALP NIKISEQQKE LVASGAGARS SSAA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR380957 Genomic DNA. Translation: CAG61522.1.
RefSeqXP_448559.1. XM_448559.1.

3D structure databases

ProteinModelPortalQ6FMI5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2890361.
KEGGcgr:CAGL0K07788g.

Phylogenomic databases

HOGENOMHOG000191209.
KOK00143.
OMAIDTHLSR.
OrthoDBEOG4BCHW2.

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.
IPR006162. PPantetheine_attach_site.
IPR010080. Thioester_reductase_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. ACP_like. 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.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYS2_CANGA
AccessionPrimary (citable) accession number: Q6FMI5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 19, 2004
Last modified: May 29, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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