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Q7M523

- 1A1D_CYBSA

UniProt

Q7M523 - 1A1D_CYBSA

Protein

1-aminocyclopropane-1-carboxylate deaminase

Gene
N/A
Organism
Cyberlindnera saturnus (Yeast) (Williopsis saturnus)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      Previous versions | rss
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    Functioni

    Catalyzes a cyclopropane ring-opening reaction, the irreversible conversion of 1-aminocyclopropane-1-carboxylate (ACC) to ammonia and alpha-ketobutyrate.

    Catalytic activityi

    1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3.

    Cofactori

    Pyridoxal phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei78 – 781Nucleophile

    GO - Molecular functioni

    1. 1-aminocyclopropane-1-carboxylate deaminase activity Source: UniProtKB-EC
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. amine catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Pyridoxal phosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1-aminocyclopropane-1-carboxylate deaminase (EC:3.5.99.7)
    Short name:
    ACC deaminase
    Short name:
    ACCD
    OrganismiCyberlindnera saturnus (Yeast) (Williopsis saturnus)
    Taxonomic identifieri907340 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeCyberlindnera

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3413411-aminocyclopropane-1-carboxylate deaminasePRO_0000184512Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylserine1 Publication
    Modified residuei51 – 511N6-(pyridoxal phosphate)lysine

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    341
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni2 – 43
    Beta strandi12 – 154
    Beta strandi18 – 203
    Helixi22 – 276
    Turni28 – 303
    Beta strandi32 – 387
    Helixi39 – 413
    Helixi50 – 556
    Turni56 – 583
    Helixi59 – 646
    Beta strandi68 – 758
    Helixi79 – 9113
    Beta strandi94 – 1007
    Helixi107 – 1093
    Turni110 – 1156
    Helixi117 – 1248
    Beta strandi128 – 1314
    Helixi142 – 15312
    Beta strandi158 – 1614
    Helixi163 – 1653
    Turni169 – 1735
    Helixi174 – 18916
    Beta strandi194 – 20310
    Helixi204 – 21310
    Helixi214 – 2163
    Helixi219 – 2213
    Beta strandi222 – 2265
    Helixi231 – 24919
    Helixi274 – 28714
    Turni293 – 2953
    Helixi296 – 30813
    Beta strandi317 – 3226
    Helixi326 – 33510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F2DX-ray2.00A/B/C/D2-341[»]
    1J0CX-ray2.75A/B/C/D1-341[»]
    1J0DX-ray2.20A/B/C/D1-341[»]
    1J0EX-ray2.45A/B/C/D1-341[»]
    ProteinModelPortaliQ7M523.
    SMRiQ7M523. Positions 1-341.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7M523.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR027278. ACCD_DCysDesulf.
    IPR005965. ACP_carboxylate_deaminase.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006278. ACCD_DCysDesulf. 1 hit.
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR01274. ACC_deam. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q7M523-1 [UniParc]FASTAAdd to Basket

    « Hide

    SGVAKFAKYP LTFGPSPISN LNRLSQHLGS KVNVYAKRED CNSGLAFGGN    50
    KLRKLEYIVP DIVEGDYTHL VSIGGRQSNQ TRMVAALAAK LGKKCVLIQE 100
    DWVPIPEAEK DVYNRVGNIE LSRIMGADVR VIEDGFDIGM RKSFANALQE 150
    LEDAGHKPYP IPAGCSEHKY GGLGFVGFAD EVINQEVELG IKFDKIVVCC 200
    VTGSTTAGIL AGMAQYGRQD DVIAIDASFT SEKTKEQTLR IANNTAKLIG 250
    VEHEFKDFTL DTRFAYPCYG VPNEGTIEAI RTCAEQEGVL TDPVYEGKSM 300
    QGLIALIKED YFKPGANVLY VHLGGAPALS AYSSFFPTKT A 341
    Length:341
    Mass (Da):37,061
    Last modified:December 15, 2003 - v1
    Checksum:i64904CDD7AA2C5FA
    GO

    Sequence databases

    PIRiPW0041.

    Cross-referencesi

    Sequence databases

    PIRi PW0041.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F2D X-ray 2.00 A/B/C/D 2-341 [» ]
    1J0C X-ray 2.75 A/B/C/D 1-341 [» ]
    1J0D X-ray 2.20 A/B/C/D 1-341 [» ]
    1J0E X-ray 2.45 A/B/C/D 1-341 [» ]
    ProteinModelPortali Q7M523.
    SMRi Q7M523. Positions 1-341.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q7M523.

    Family and domain databases

    InterProi IPR027278. ACCD_DCysDesulf.
    IPR005965. ACP_carboxylate_deaminase.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006278. ACCD_DCysDesulf. 1 hit.
    SUPFAMi SSF53686. SSF53686. 1 hit.
    TIGRFAMsi TIGR01274. ACC_deam. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Properties, sequence, and synthesis in Escherichia coli of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus."
      Minami R., Uchiyama K., Murakami T., Kawai J., Mikami K., Yamada T., Yokoi D., Ito H., Matsui H., Honma M.
      J. Biochem. 123:1112-1118(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE, CHARACTERIZATION, ACETYLATION AT SER-1.
    2. "Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus."
      Yao M., Ose T., Sugimoto H., Horiuchi A., Nakagawa A., Wakatsuki S., Yokoi D., Murakami T., Honma M., Tanaka I.
      J. Biol. Chem. 275:34557-34565(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    3. "Reaction intermediate structures of 1-aminocyclopropane-1-carboxylate deaminase: insight into PLP-dependent cyclopropane ring-opening reaction."
      Ose T., Fujino A., Yao M., Watanabe N., Honma M., Tanaka I.
      J. Biol. Chem. 278:41069-41076(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).

    Entry informationi

    Entry namei1A1D_CYBSA
    AccessioniPrimary (citable) accession number: Q7M523
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 52 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3