ID A0A3Q1I835_ANATE Unreviewed; 510 AA.
AC A0A3Q1I835;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000000696.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000000696.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q1I835; -.
DR Ensembl; ENSATET00000000710.2; ENSATEP00000000696.2; ENSATEG00000000475.2.
DR GeneTree; ENSGT00940000156110; -.
DR Proteomes; UP000265040; 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:UP000265040}.
FT DOMAIN 23..487
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 510 AA; 55426 MW; D0E10495AA77E10B CRC64;
MANSRLQIFR APPTTKLFIN GKFVESRSSE WLDIHNPATN EVIARVPKAT QEEMLAAVDS
CSTAFHSWSE TSILARQQIF LRYQQLIKDN LKELAKAITL EQGKTLADAE GDVFRGLQVV
EHACSITSLM LGETLPSITK DMDTYTYRLP LGVCAGIAPF NFPAMIPLWM FPMGMVCGNT
YLLKPSERVP TCTMLLARML QDAGAPDGTL NIIHGQHDAV NFICDHPAIK AISFVGSNQA
GEYIYERGSK NGKRVQANMG AKNHGVVMPD ANKENTLNQL VGAAFGAAGQ RCMALSTAIL
VGEAQSWLPE LVERAKHLCV NAGDQPGADV GPLISRQARE RVCSLIQSGV DEGAKLLLDG
RNIKVKGYEN GNFVGPTILG NVTPEMKCYT EEIFGPVLVV LEADSLDDAI SLVNRSPYGN
GTAIFTTNGA TARKYTHKVD VGQVGVNVPI PVPLPMFSFT GSRGSFRGDM NFYGKQGIQF
YTQIKTVTSQ WKAEDATLKS PAVTMPTMGR
//
