(data stored in ACNUC5340 zone)

HOGENOM: AEDAE_1446_PE9

ID   AEDAE_1446_PE9                       STANDARD;      PRT;   521 AA.
AC   AEDAE_1446_PE9; Q17M80;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Probable methylmalonate-semialdehyde dehydrogenase
DE   (AEDAE_1446.PE9) [acylating], mitochondrial; Short=MMSDH;
DE   Short=Malonate-semialdehyde dehydrogenase [acylating]; EC=1.2.1.18;
DE   EC=1.2.1 27;Flags: Precursor; .
GN   ORFNames=AAEL001134;
OS   AEDES AEGYPTI.
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera;
OC   Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; Culicinae;
OC   Culicini; Aedes.
OX   NCBI_TaxID=7159;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AEDAE_1446.PE9.
CC       Aedes aegypti supercontig supercont1.23 AaegL1  sequence 1..3969038
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:MMSA_AEDAE
CC   -!- FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds
CC       fatty acyl-CoA (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-methyl-3-oxopropanoate + CoA + H(2)O +
CC       NAD(+) = propanoyl-CoA + HCO(3)(-) + NADH.
CC   -!- CATALYTIC ACTIVITY: 3-oxopropanoate + CoA + NAD(P)(+) = acetyl-CoA
CC       + CO(2) + NAD(P)H.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC   -!- GENE_FAMILY: HOG000271507 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Aedes_aegypti;AAEL001134;AAEL001134-RA;AAEL001134-PA.
DR   EMBL; CH477208; - ;
DR   UniProtKB/Swiss-Prot; Q17M80; -.
DR   EMBL; CH477208; EAT47764.1; -; Genomic_DNA.
DR   RefSeq; XP_001652386.1; XM_001652336.1.
DR   UniGene; Aae.2920; -.
DR   ProteinModelPortal; Q17M80; -.
DR   STRING; Q17M80; -.
DR   EnsemblMetazoa; AAEL001134-RA; AAEL001134-PA; AAEL001134.
DR   GeneID; 5568558; -.
DR   KEGG; aag:AaeL_AAEL001134; -.
DR   VectorBase; AAEL001134; Aedes aegypti.
DR   eggNOG; inNOG06001; -.
DR   GeneTree; EMGT00050000005689; -.
DR   OMA; KHIYERG; -.
DR   OrthoDB; EOG4N5TC3; -.
DR   PhylomeDB; Q17M80; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; ISS:UniProtKB.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; ISS:UniProtKB.
DR   GO; GO:0019859; P:thymine metabolic process; ISS:UniProtKB.
DR   GO; GO:0006573; P:valine metabolic process; ISS:UniProtKB.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR010061; MeMal-semiAld_DH.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699:SF27; MMSDH; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   TIGRFAMs; TIGR01722; MMSDH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
DR   HOGENOMDNA; AEDAE_1446.PE9; -.
KW   AAEL0011343; AAEL001134-PA ; Q17M80; CH477208;
KW   Mitochondrion; NAD; Oxidoreductase; Transit peptide.
SQ   SEQUENCE   521 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MALVRLLGVE CRNALQRSYS TASVPTTKMF IDGKFVDSKT TEWIDLHDPA TNKVVTRVPK
     CTQDEMESAV ESSKKAFKTW SQTSILGRQQ VMFKLQHLIR NNMSELAKNI TKEQGKTLVD
     AEGDVLRGLQ VVEHCCSITS LQMGETVPNI AKDMDTYSYT LPLGVTAGIC PFNFPAMIPL
     WMFPVAITCG NTSIIKPSER VPGATMMLME LLNEAGCPPG VVNVIHGAHD AVNFICDNPT
     IKAVSFVGSD QAGKYIYERA GRNGKRVQSN MGAKNHGVIM ADANKENTLN QLAGAAFGAA
     GQRCMALSTA VFVGEAKQWI PDLVERARKL KVNAGHVPGT DVGPVISPQS KQRINELVES
     GVKEGAKLVL DGRSIKVENF ENGNFVGPTI LTDVSTNMKC YTEEIFGPVL VCLTVDTVDE
     AVEMINNNPY GNGTAIFTTN GATARKFVNE IDVGQVGVNV PIPVPLPMFS FTGSRGSFMG
     DCHFYGKQGV KFYTQTKTVT QLWREGDVSH TKAAVAMPTM K
//

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