ID A0A1W4WMT8_AGRPL Unreviewed; 520 AA.
AC A0A1W4WMT8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 Name=LOC108734334 {ECO:0000313|RefSeq:XP_018321364.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018321364.1};
RN [1] {ECO:0000313|RefSeq:XP_018321364.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_018321364.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_018321355.1; XM_018465853.1.
DR RefSeq; XP_018321364.1; XM_018465862.2.
DR AlphaFoldDB; A0A1W4WMT8; -.
DR STRING; 224129.A0A1W4WMT8; -.
DR EnsemblMetazoa; XM_018465862.2; XP_018321364.1; LOC108734334.
DR GeneID; 108734334; -.
DR KEGG; apln:108734334; -.
DR InParanoid; A0A1W4WMT8; -.
DR OrthoDB; 275238at2759; -.
DR Proteomes; UP000192223; Unplaced.
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:UP000192223}.
FT DOMAIN 36..499
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 520 AA; 56349 MW; CBC7F5B3A013D8BA CRC64;
MSLPRTSISP LLKAFNRTYS SNVAPTTKLF IDGKFQESQT TEWIDLHDPA TNELVTKVPK
TTQAEMQAAV ESSRKAYESW KDTTVLTRQQ LMLKFQAVIR RDIKKLAENI TKEQGKTLVD
AEGDVFRGLQ VVEHSCAAGT LLQGESLNNI AKDVDCVSYK LPLGVVAGIC PFNFPAMIPL
WMAPLALIAG NTCIIKPSER DPGATMLLME LLNEVGCPPG VVNIIHGSHD AVNFICDSPD
IKAISFVGST NAGKYIYSRA SATGKRVQSN MGAKNHAIVL PDANKDMAID HLLGAAFGAA
GQRCMAISVA ILVGDAKSWI PEIVERSKRL KVSAGYEPGA DIGPVISPQA KSKIVDLITS
GIKQGAKCVL DGRNIKVEKY PKGNFVGPTI LTEVQTDFEC YQEEIFGPVL SVMFADTLDD
AIEIINKNPY GNGAAIFTTN GSHARQFVNE VDAGQVGVNV PIPVPLPMFS FTGSRGSFYG
DLHFYGKQGL NFYTQTKTIT SLWRKGQAVS RPSVSMPVHH
//
