(data stored in ACNUC7421 zone)

SWISSPROT: Q2IMX6_ANADE

ID   Q2IMX6_ANADE            Unreviewed;       362 AA.
AC   Q2IMX6;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   13-FEB-2019, entry version 81.
DE   SubName: Full=Aspartate semialdehyde dehydrogenase {ECO:0000313|EMBL:ABC80158.1};
DE            EC=1.2.1.11 {ECO:0000313|EMBL:ABC80158.1};
GN   OrderedLocusNames=Adeh_0382 {ECO:0000313|EMBL:ABC80158.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80158.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase
CC       family. {ECO:0000256|SAAS:SAAS00827794}.
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DR   EMBL; CP000251; ABC80158.1; -; Genomic_DNA.
DR   RefSeq; WP_011419441.1; NC_007760.1.
DR   STRING; 290397.Adeh_0382; -.
DR   EnsemblBacteria; ABC80158; ABC80158; Adeh_0382.
DR   KEGG; ade:Adeh_0382; -.
DR   eggNOG; ENOG4107QK3; Bacteria.
DR   eggNOG; COG0136; LUCA.
DR   HOGENOM; HOG000013358; -.
DR   KO; K00133; -.
DR   OMA; WPEMVDN; -.
DR   BioCyc; ADEH290397:G1G5W-392-MONOMER; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00978; asd_EA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q2IMX6.
DR   SWISS-2DPAGE; Q2IMX6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Oxidoreductase {ECO:0000313|EMBL:ABC80158.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935}.
FT   DOMAIN        7    139       Semialdhyde_dh. {ECO:0000259|SMART:
FT                                SM00859}.
SQ   SEQUENCE   362 AA;  39310 MW;  6F57A3E27E11B730 CRC64;
     MSQKKLKVGV LGATGMVGQR FVALLEHHPW YEVTLVAASA NSAGQKYADA VKGRWALRSA
     LPAATAGLTV KNASDVAAIA GEVDFVFCAV DMPKDETARL EEDYAKHETP VVSNNSAHRG
     TADVPMMVPE LNPEHAAVIE AQRRRLGTSR GFIAVKPNCS LQSYVPAIHP LMKFGPKRIA
     VATYQAISGA GKTFESWPEM VDNLIPFIKG EEEKSEKEPM KIWGRVEGGK IVAAQDPVIT
     AQCIRVPASD GHMAAVFVSF ERKPSKDDVL ELWRSFSGKP QKLGLPSAPK PFLQYFEDES
     RPQTRLDRDA GNGMAVTIGR LRPDAIFDWR FVCLSHNTVR GAAGGAVLTA ELLTADGYIQ
     AK
//

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