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Q12572

- LYS2_CANAX

UniProt

Q12572 - LYS2_CANAX

Protein

L-aminoadipate-semialdehyde dehydrogenase large subunit

Gene

LYS2

Organism
Candida albicans (Yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (15 Jul 1999)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    Binds 1 phosphopantetheine covalently.Curated

    Pathwayi

    GO - Molecular functioni

    1. L-aminoadipate-semialdehyde dehydrogenase activity Source: UniProtKB-EC
    2. phosphopantetheine binding Source: InterPro

    GO - Biological processi

    1. lysine biosynthetic process via aminoadipic acid Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Amino-acid biosynthesis, Lysine biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    UniPathwayiUPA00033; UER00032.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-aminoadipate-semialdehyde dehydrogenase large subunit (EC:1.2.1.31)
    Alternative name(s):
    Alpha-aminoadipate reductase
    Short name:
    Alpha-AR
    Gene namesi
    Name:LYS2
    OrganismiCandida albicans (Yeast)
    Taxonomic identifieri5476 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13911391L-aminoadipate-semialdehyde dehydrogenase large subunitPRO_0000193149Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei884 – 8841O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ12572.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini852 – 90251Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3320.

    Family and domain databases

    Gene3Di1.10.1200.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProiIPR010071. 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]
    PfamiPF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    PF07993. NAD_binding_4. 1 hit.
    PF00550. PP-binding. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001617. Alpha-AR. 1 hit.
    SUPFAMiSSF47336. SSF47336. 1 hit.
    TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
    TIGR03443. alpha_am_amid. 1 hit.
    TIGR01746. Thioester-redct. 1 hit.
    PROSITEiPS50075. ACP_DOMAIN. 1 hit.
    PS00455. AMP_BINDING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12572-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDFWLNYLD NPTLSVLPHD FLKPANNKSV EGTYTFNIDN GSTDFKFGLA     50
    VFAALVYRLT GDEDIVIATD ESANTPEFIV RLNLTPELTF QELVSKITKE 100
    YENNISQINY KALSEVSHRI KEAKGLDENP GLFRLSYQHA HSNQQLNTTV 150
    EGSIRDLAIY TDGTKFTIYY NALLYSHERV VICGEQFAQL TTVSGDTDTV 200
    IAEVFLITDF HKKNLPDPTI DLDWSGYRGA IQEIFMDNAN KHPDRTCVVE 250
    TVSFLESNSK TRNFSYHKLI KLLIVVGNYL KETGIKKGDI VMIYAYRGVD 300
    LMIAVMGVLK AGATFSVIDP AYPPARQNIY LSVAKPKGLI GLEKAGTLDQ 350
    LVVDYISNEL DVVSTIPQLK VQDDGTLVGG KLEGADNDCL NDYQKFKDQP 400
    AGVIVGPDSR PTLSFTSGSE GIPKGVLGRH YSLAYYFPWM AKRFRLSEKD 450
    KFTILSGIAH DPIQRDMFTP LFLGAQLLVP TADDIGTPGK LADWMAKYGA 500
    TVTHLTLAMG QLLSAQATTA IPSLHAFFVG DILTKRDCLR LQSLAENVFI 550
    VNMLWSLSQT QRSVSYFEIK SRKADPTYLK NLKAVMPAGT GMHNVQLLVV 600
    NRNDRSQTCG VGEVGEIYVR AAGLAEGYRG LPDLNAAKFI TNWYVNPDKW 650
    IEQDEANKKS SETSERTWSV KPRDRMYRSG DLGRYFSDGN VECCGRADDQ 700
    VKIRGFRIEL GEIDTHLSQH PLVRENVTLV RRDKNEEPTL ISYIVPKDSP 750
    ELKTFFADVD FPLKKSNDPI VKGLVAYREL IKDIKGYLKK KLASYAIPTI 800
    IVPLVKLPLN PNGKVDKPKL PFPDTAQLAA VAKLSVSSHD AQAAEEENLT 850
    KLEEQIRDLW LDVLPNRPAT ISKDDSFFDL GSHSILGTRI FTYEQKLNVE 900
    IPLVSFKGDQ RRPRFPIGLS RYNYSRREQR CRRFLKAKTY TMRRSKELSK 950
    ELSKSALLES YSSLKQLPSG SVNVFVTGAT GFLGSFIVRD LLTARNKNLD 1000
    IKVYAHVRAS SKEAGLQRLR QTGITYGIWD ENWAEKIEIV LGDLSKEKFG 1050
    LDNSQWSDLT NSIDVLFTMV LCHWVYPYSQ LRMLNVIGTI NVFNMAGEVK 1100
    LKFFSFVSST SALDTDYFVN LSDELLAQGK NGISEADDLQ GSAKGLGNGY 1150
    GQSKWAAEYI IRRAGERGLK GCITRPGYVA GFSKTGASNT DDFLLRMLKG 1200
    SAELGLYPDI TNNVNMVPVD HVARVVTATA LNPPSSEELT VAHVTGHPRI 1250
    LFNNFLGCLK AYGYEINPAD YPVWTSALEK FVIEESKESA LFPLLHFVLD 1300
    NLPQDTKAPE LDDSNAAKSL KQDSKYTGED FSAGKGVDLD QTGVYISYLI 1350
    KIGFLPKPTG TGEKKLPEVE ISDESLKLIS GGAGARGSAA K 1391
    Length:1,391
    Mass (Da):154,741
    Last modified:July 15, 1999 - v2
    Checksum:iB7E641866235BCDD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58133 Genomic DNA. Translation: AAC02241.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58133 Genomic DNA. Translation: AAC02241.1 .

    3D structure databases

    ProteinModelPortali Q12572.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG3320.

    Enzyme and pathway databases

    UniPathwayi UPA00033 ; UER00032 .

    Family and domain databases

    Gene3Di 1.10.1200.10. 1 hit.
    3.40.50.720. 1 hit.
    InterProi IPR010071. 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 ]
    Pfami PF00501. AMP-binding. 1 hit.
    PF13193. AMP-binding_C. 1 hit.
    PF07993. NAD_binding_4. 1 hit.
    PF00550. PP-binding. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001617. Alpha-AR. 1 hit.
    SUPFAMi SSF47336. SSF47336. 1 hit.
    TIGRFAMsi TIGR01733. AA-adenyl-dom. 1 hit.
    TIGR03443. alpha_am_amid. 1 hit.
    TIGR01746. Thioester-redct. 1 hit.
    PROSITEi PS50075. ACP_DOMAIN. 1 hit.
    PS00455. AMP_BINDING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiLYS2_CANAX
    AccessioniPrimary (citable) accession number: Q12572
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3