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Q7M181

- ACLR_ACHOB

UniProt

Q7M181 - ACLR_ACHOB

Protein

2-aminohexano-6-lactam racemase

Gene
N/A
Organism
Achromobacter obae
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (15 Dec 2003)
      Previous versions | rss
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    Functioni

    catalyzes the interconversion of L-alpha-amino-epsilon-caprolactam and D-alpha-amino-epsilon-caprolactam.1 Publication

    Catalytic activityi

    (S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam.1 Publication

    Cofactori

    Pyridoxal phosphate.Curated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei137 – 13711 Publication
    Binding sitei137 – 1371Pyridoxal phosphateBy similarity
    Binding sitei295 – 2951Pyridoxal phosphate1 Publication

    GO - Molecular functioni

    1. pyridoxal phosphate binding Source: InterPro
    2. transaminase activity Source: InterPro

    Keywords - Molecular functioni

    Isomerase

    Keywords - Ligandi

    Pyridoxal phosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-aminohexano-6-lactam racemase (EC:5.1.1.15)
    Alternative name(s):
    2-amino-hexano-6-lactam racemase
    Alpha-amino-epsilon-caprolactam racemase
    OrganismiAchromobacter obae
    Taxonomic identifieri37486 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAchromobacter

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4364362-aminohexano-6-lactam racemasePRO_0000430444Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei267 – 2671N6-(pyridoxal phosphate)lysine

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZUKX-ray2.41A/B1-436[»]
    3DXVX-ray2.21A/B1-436[»]
    3DXWX-ray2.41A/B1-436[»]
    ProteinModelPortaliQ7M181.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7M181.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni110 – 1112Pyridoxal phosphate binding
    Regioni238 – 2414Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11986. PTHR11986. 1 hit.
    PfamiPF00202. Aminotran_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7M181-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKALYDRDG AAIGNLQKLR FFPLAISGGR GARLIEENGR ELIDLSGAWG    50
    AASLGYGHPA IVAAVSAAAA NPAGATILSA SNAPAVTLAE RLLASFPGEG 100
    THKIWFGHSG SDANEAAYRA IVKATGRSGV IAFAGAYHGC TVGSMAFSGH 150
    SVQADAAKAD GLILLPYPDP YRPYRNDPTG DAILTLLTEK LAAVPAGSIG 200
    AAFIEPIQSD GGLIVPPDGF LRKFADICRA HGILVVCDEV KVGLARSGRL 250
    HCFEHEGFVP DILVLGKGLG GGLPLSAVIA PAEILDCASA FAMQTLHGNP 300
    ISAAAGLAVL ETIDRDDLPA MAERKGRLLR DGLSELAKRH PLIGDIRGRG 350
    LACGMELVCD RQSREPARAE TAKLIYRAYQ LGLVVYYVGM NGNVLEFTPP 400
    LTITETDIHK ALDLLDRAFS ELSAVSNEEI AQFAGW 436
    Length:436
    Mass (Da):45,699
    Last modified:December 15, 2003 - v1
    Checksum:i85D1FC7936F7DDE5
    GO

    Sequence databases

    PIRiJC1497.

    Cross-referencesi

    Sequence databases

    PIRi JC1497.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZUK X-ray 2.41 A/B 1-436 [» ]
    3DXV X-ray 2.21 A/B 1-436 [» ]
    3DXW X-ray 2.41 A/B 1-436 [» ]
    ProteinModelPortali Q7M181.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q7M181.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11986. PTHR11986. 1 hit.
    Pfami PF00202. Aminotran_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alpha-amino-epsilon-caprolactam racemase for L-lysine production."
      Naoko N., Oshihara W., Yanai A.
      (In) Korpela T., Christen P. (eds.); Biochemistry of Vitamin B6, pp.449-452, Birkhauser Verlag, Basel (1987)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Mechanism of alpha-amino-epsilon-caprolactam racemase reaction."
      Ahmed S.A., Esaki N., Tanaka H., Soda K.
      Biochemistry 25:385-388(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    3. "Finding Sequences for over 270 Orphan Enzymes."
      Shearer A.G., Altman T., Rhee C.D.
      PLoS ONE 9:E97250-E97250(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    4. "The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae."
      Okazaki S., Suzuki A., Mizushima T., Kawano T., Komeda H., Asano Y., Yamane T.
      Biochemistry 48:941-950(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND EPSILON-CAPROLACTAM, PYRIDOXAL PHOSPHATE AT LYS-267, ACTIVE SITE, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiACLR_ACHOB
    AccessioniPrimary (citable) accession number: Q7M181
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 2014
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 46 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic 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