(data stored in SCRATCH zone)

SWISSPROT: Q13R42_PARXL

ID   Q13R42_PARXL            Unreviewed;       511 AA.
AC   Q13R42;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 79.
DE   SubName: Full=Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase {ECO:0000313|EMBL:ABE33447.1};
DE            EC=1.2.99.3 {ECO:0000313|EMBL:ABE33447.1};
GN   ORFNames=Bxe_B2545 {ECO:0000313|EMBL:ABE33447.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33447.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33447.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33447.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; CP000271; ABE33447.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q13R42; -.
DR   STRING; 266265.Bxe_B2545; -.
DR   EnsemblBacteria; ABE33447; ABE33447; Bxe_B2545.
DR   KEGG; bxe:Bxe_B2545; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271505; -.
DR   KO; K09472; -.
DR   OMA; CHEALFF; -.
DR   OrthoDB; POG091H05FS; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13R42.
DR   SWISS-2DPAGE; Q13R42.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345,
KW   ECO:0000313|EMBL:ABE33447.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       49    507       Aldedh. {ECO:0000259|Pfam:PF00171}.
SQ   SEQUENCE   511 AA;  54225 MW;  BF67CD4264A0EA66 CRC64;
     MRNTQFTQIS RSFVVNIPDA SVWRARAQEI RPEGRAFIDG NYVGALSGRT FATVNPATGQ
     VIAQVAECGE EDVNLAVASA RKAFESGVWS RRAPAERKAV MLRFAQLMME HREELALLES
     LDVGKPVANA YNGDIVSSAT CIQWYGEAID KLYGETAPAA PDMTTMIVRE PLGVVAAVVP
     WNYPLSMASW KLGPALAAGN SVVLKPAEQS PLSAIRIAAL AMEAGLPAGV LNVLPGYGET
     AGRALGLHMD VDAVGFTGST AVGKLFMQYS GQSNIKRVGL ECGGKSPHIV LDDCADLDAA
     ARAVAAGIFG NSGQVCNAGS RLIVQAAVRD ELLEKVAAIA RELVPGDPLD PATKMGAIVS
     DVQHASIMSY IDAGRADGAR VVAGGRAARP ESGGYFIEPT VFDGVNNDMR IAREEIFGPV
     LSAITVDSPE EAVRVANDTI YGLAAAVWTS NVTRAQQVSR QLKAGVVWVN CFDRGTMSSP
     FGGFKQSGFG RDKSMHAFDK YMDWKAIWIA G
//

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