ID A0A195CVX7_9HYME Unreviewed; 559 AA.
AC A0A195CVX7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Probable methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial {ECO:0000256|ARBA:ARBA00039517};
DE EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
DE AltName: Full=Malonate-semialdehyde dehydrogenase [acylating] {ECO:0000256|ARBA:ARBA00042419};
GN ORFNames=ALC62_05075 {ECO:0000313|EMBL:KYN04309.1};
OS Cyphomyrmex costatus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Cyphomyrmex.
OX NCBI_TaxID=456900 {ECO:0000313|EMBL:KYN04309.1, ECO:0000313|Proteomes:UP000078542};
RN [1] {ECO:0000313|EMBL:KYN04309.1, ECO:0000313|Proteomes:UP000078542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS0001 {ECO:0000313|EMBL:KYN04309.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN04309.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Cyphomyrmex costatus WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable malonate and methylmalonate semialdehyde
CC dehydrogenase involved in the catabolism of valine, thymine, and
CC compounds catabolized by way of beta-alanine, including uracil and
CC cytidine. {ECO:0000256|ARBA:ARBA00037458}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) +
CC hydrogencarbonate + NADH + propanoyl-CoA; Xref=Rhea:RHEA:20804,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57700, ChEBI:CHEBI:57945; EC=1.2.1.27;
CC Evidence={ECO:0000256|ARBA:ARBA00036429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20805;
CC Evidence={ECO:0000256|ARBA:ARBA00036429};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + CoA + H2O + NAD(+) = acetyl-CoA + H(+) +
CC hydrogencarbonate + NADH; Xref=Rhea:RHEA:76615, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.27;
CC Evidence={ECO:0000256|ARBA:ARBA00036793};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76616;
CC Evidence={ECO:0000256|ARBA:ARBA00036793};
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DR EMBL; KQ977279; KYN04309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195CVX7; -.
DR STRING; 456900.A0A195CVX7; -.
DR Proteomes; UP000078542; Unassembled WGS sequence.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IEA:UniProtKB-EC.
DR CDD; cd07085; ALDH_F6_MMSDH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR010061; MeMal-semiAld_DH.
DR NCBIfam; TIGR01722; MMSDH; 1.
DR PANTHER; PTHR43866; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43866:SF3; METHYLMALONATE-SEMIALDEHYDE DEHYDROGENASE [ACYLATING], MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000078542}.
FT DOMAIN 75..537
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 559 AA; 60633 MW; 37BF1265033E7373 CRC64;
MPRRLNARPF FRYESFSSTQ AAPTNVLTES MALLARIVKC EVRIYTSPSR STRFARSYCN
AVPAVKIYID GQIVESKATE FTNVHDPATN QLLYRTPKCT RDEMESAVQS AQKAYEKWRH
TSVLTRQNLM LKYQALIREH SKDIAVNLVR ENGKTLADAE GDVLRGLQVV DACTSIPMLQ
MGESTTNIAT DMDIISYKVP LGVTASICPF NFPAMIPLWS FPISVACGNA AILKPSERVP
GASMILADLF TKAGAPAGLL NVIHGQHAAV DFICEHPDIK AVSFVGSDQA GKYIYKQSTA
HGKRVQCNMG AKNHCVVLPD ANKNKTLSQI TGAAFGAAGQ RCMALSVAIF VGKSKEWIPE
LVEAAKKLKV NAGHVPGTDL GPVISPQAKQ RIIELVESGV RDGAKLPLDG RGIVVSGFEN
GNFVGPTVLT DVKPTMKCYT EEIFGPVLSC MFTDTTDEAI DIINKNPYGN GTAVFTTNGA
TARAFVNRIE AGQVGVNVPI PVPLPMFSFT GNKGSFLGDM NFYGKYGVNF HTQTKTITQL
WRSDDATDIA SSTAMPTMQ
//
