ID A0A194RRW7_PAPMA Unreviewed; 1128 AA.
AC A0A194RRW7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=RR48_07530 {ECO:0000313|EMBL:KPJ20065.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ20065.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ20065.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ20065.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ20065.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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};
CC -!- SIMILARITY: Belongs to the DNase II family.
CC {ECO:0000256|ARBA:ARBA00007527}.
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DR EMBL; KQ459765; KPJ20065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194RRW7; -.
DR STRING; 76193.A0A194RRW7; -.
DR InParanoid; A0A194RRW7; -.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004531; F:deoxyribonuclease II activity; IEA:InterPro.
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 CDD; cd09121; PLDc_DNaseII_2; 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; IPR004947; DNase_II.
DR InterPro; IPR010061; MeMal-semiAld_DH.
DR PANTHER; PTHR43866; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR43866:SF3; METHYLMALONATE-SEMIALDEHYDE DEHYDROGENASE [ACYLATING], MITOCHONDRIAL; 1.
DR Pfam; PF00171; Aldedh; 2.
DR Pfam; PF03265; DNase_II; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 158..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..308
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 333..471
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 1128 AA; 125476 MW; 5FEEAAC371302154 CRC64;
MLKVFKNESR LIFNRSYSSS APSTKLYIDG QFVESKTNNW IELTNPATNE VIGRVPETTK
EELNTALEAA KKAYKPWSQS TVMTRQQLMF KFARLLRENQ SKLAAKITEE QGKTTADAEG
DVLRGIQLVE HCCSITSLQL GDCIQNIAKD MDTHSYKVPL GVVGGVAAFN FPVMIPLWMF
PPALVTGNTC LVKPSEQDPG ATLMMMELLQ EAGAPPGVVN VIHGTHDPVN FICDHPDIKA
VSFVGGDGAG KHIYTRASAA GKRVQSNMGA KNHGVILPDA NKEHTLNQLT GAAFGAAGQR
CMALSTAVFV GEAKEWIPDL EFDSLIQVYK FSRVKDGAKL VLDGRGIKVS GFEKGNFVGP
TILTDVKPNM ECYKEEIFGP VLICLFVDTL DEAIQMINSN PYGNGTAIFT TNGAAARKFS
AEIDVGQVGV NVPIPVPLSM FSFTGTRGSF LGTNHFCGKQ GKDFYTELKT VVSFWRQSDV
SHTKAADRNI ISLVYNDQPP ATEHQPDILQ SVAEMYSKSK RGQMNQAGVK KFKKFKLGDK
YYDDYDLAEM CKMHSKFMKS RVESGHTKGV ILGDKFTALW LVHSVPRFPP LPDIHGLNVS
SYNYPTTGTK YGQSFLCVSV QTSTLNQIAT QLKYNEPLIV YYHMPPDFDS ELPNLVDVVH
NKTIDASPWY HIESFETLVG RKFLSFAKSA MFNDDLYSGL VAEVLQSDLL VESWTNGPGT
LDSEYTRNFQ VRNIERLKFP IAKMSFTSHN DHSKWAVAVA HKMHNSQDTK VADYWVCVGD
INRALPQESR GGGTVCTSGP ILWGNFAHLI ESVQTWYIYK PPSDIAPYLE LGRNFTYITS
RNAGRWQPSS KYITANSMLQ HTLSPIYRPT YTDYLAVAVY EPRSTSEARG VLLADEVGGV
WIGHTVPGLI DMRDDRPTFP DSERANGHLL MCLSIDLLAI NEIASALQVA APMFSYVKVP
KRMRELLPSW DFQHDTNSKE KQTKKVNFLT NSEHLTVEML ARPPANEGSL YEEFAASKEL
VLDVYSPTDG EYLSSVCAKN FSVRNIETIS LKLKESVQYV SNLSDRTRFA VSTAASWQKM
KSLPPQYWTC VSNLDKEDTT GKGGLITCVD DYSIWLTFDN FKVKEPEC
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