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O74298

- LYS2_PENCH

UniProt

O74298 - LYS2_PENCH

Protein

L-aminoadipate-semialdehyde dehydrogenase large subunit

Gene

lys2

Organism
Penicillium chrysogenum (Penicillium notatum)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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
    OrganismiPenicillium chrysogenum (Penicillium notatum)
    Taxonomic identifieri5076 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicilliumPenicillium chrysogenum complex

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14091409L-aminoadipate-semialdehyde dehydrogenase large subunitPRO_0000193151Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei896 – 8961O-(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

    ProteinModelPortaliO74298.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini863 – 93472Acyl carrierPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 acyl carrier domain.PROSITE-ProRule annotation

    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.

    O74298-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVGTASLQD RLETWAQRLK NLTVSPLTRD YPDTQKTDSK RVIEAFESLQ     50
    LPKAKLTGSS SSFIAFLTAF IILVARLTGD EDIAVGTNSN EDGRAFVIRV 100
    PIDTSESFAQ LYAKVDKAYK EGSSQIVPLG SLRSYIQEKS KSERTPVLFR 150
    FAAYDAPASS QDYPANTFDT TDLVVNVAPG SAEVELGAYY NQRLFSSARI 200
    AFILKQLASI ASNAAANPDE AIGRIDLMTE DQRALLPDPT CNLNWSNFRG 250
    AIHDIFTANA ERHPEKLCVV ETQSSSSPHR EFTYRQINEA SNILGHHLVR 300
    SGIQRGEVVM VYAYRGVDLV VAVMGILKAG ATFSVIDPAY PPERQNIYLD 350
    VARPRALVNI AKATKDAGEL SDIVRTFIDE NLELRTEIPA LALLDDGTLA 400
    GGSINGQDVF ANDVALKSKP TGVVVGPDSI PTLSFTSGSE GRPKGVRGRH 450
    FSLAYYFPWM SETFKLTPDE KFTMLSGIAH DPIQRDIFTP LFLGAQLLVP 500
    AREDIQNEKL AEWIEKYGAT ITHLTPAMGQ ILVGGASAQF PALHHAFFVG 550
    DILIKRDCRS LQGLAPNVSI VNMYGTTETQ RAVSYYEIPS YASNEGYLNN 600
    MKDVIMAGRG MLDVQMLVVN RYDPTRLCAI GEVGEIYVRA GGLAEGYLGS 650
    PELSAKKFLN NWFVNPEIWA EKDQAESRNE PWRQFYVGPR DRLYRSGDLG 700
    RYTPSGDVEC SGRADDQVKI RGFRIELGEI DTHLSQHPLV RENVTLVRRD 750
    KDEEPTLVSY FVPDMNKWAS WLESKGLKDD DSDSEGMVGL LRRFRPLRDD 800
    AREHLRTKLP TYAVPTVIIP LKRMPLNPNG KIDKPALPFP DTAELSAAAP 850
    RRASSALQAL SETEQTLAQV WAKLIPNVTS RMIGPDDSFF DLGGHSILAQ 900
    QMFFELRRKW RVIDISMNAI FRSPTLKGFA SEIDRLLAME SFATSDDKTL 950
    AVQAANEPDD EYSKDAVQLV NELPKTFPQR TEAMLTSEPT VFLTGATGFL 1000
    GAHILRDLLT RKSPSTKVVA LVRAKTEELA LERLRSTCRA YGFWDEAWTA 1050
    KLQAVCGDLG KPQFGLSQSV WDDLTNRVDA VIHNGALVHW VYPYATLRPA 1100
    NVMGTIDALK LCASGKAKQF AFVSSTSALD KDRYVQESER IIAAGGNGIS 1150
    EDDDMEGSRV GLGTGYGQSK WAGEYLVKEA GRRGLRGTIV RSGYVLGDSV 1200
    TGTTNTDDFL IRMLKGCIQI GLRPNIFNTV NMVPVDHVAR IVIATAFHPP 1250
    ATGVNVAHVT GHPRLRFNQF LGALELYGYN VPQVDYVPWS TSLEQYVNDG 1300
    EHNDKESQHA LMPLYHFVTS DLPSNTKAPE LDDVNAATAL RADATWSGVD 1350
    ASAGAGVTEE LVGLYASYLV QTGFLPAPTV AGARPLPAAQ ISEEQKKTLL 1400
    SVGGRGGTS 1409
    Length:1,409
    Mass (Da):154,842
    Last modified:November 1, 1998 - v1
    Checksum:iA85DFD397BAB29AE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13967 Genomic DNA. Translation: CAA74300.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y13967 Genomic DNA. Translation: CAA74300.1 .

    3D structure databases

    ProteinModelPortali O74298.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Characterization of the lys2 gene of Penicillium chrysogenum encoding alpha-aminoadipic acid reductase."
      Casqueiro J., Gutierrez S., Banuelos O., Fierro F., Velasco J., Martin J.F.
      Mol. Gen. Genet. 259:549-556(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: AS-P-78.

    Entry informationi

    Entry nameiLYS2_PENCH
    AccessioniPrimary (citable) accession number: O74298
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 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