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Database: UniProt
Entry: A0A401SV95_CHIPU
LinkDB: A0A401SV95_CHIPU
Original site: A0A401SV95_CHIPU 
ID   A0A401SV95_CHIPU        Unreviewed;       523 AA.
AC   A0A401SV95;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE            EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
GN   ORFNames=chiPu_0012792 {ECO:0000313|EMBL:GCC34319.1};
OS   Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC   Chiloscyllium.
OX   NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC34319.1, ECO:0000313|Proteomes:UP000287033};
RN   [1] {ECO:0000313|EMBL:GCC34319.1, ECO:0000313|Proteomes:UP000287033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA   Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA   Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA   Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA   Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT   "Shark genomes provide insights into elasmobranch evolution and the origin
RT   of vertebrates.";
RL   Nat. Ecol. Evol. 2:1761-1771(2018).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GCC34319.1}.
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DR   EMBL; BEZZ01000588; GCC34319.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401SV95; -.
DR   STRING; 137246.A0A401SV95; -.
DR   OMA; HGKRAQC; -.
DR   Proteomes; UP000287033; 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:UP000287033}.
FT   DOMAIN          37..500
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   523 AA;  56778 MW;  31CE2B8727A4494B CRC64;
     MAAVLRVALR RKITPPLGCM CYSSPPTTKL FIDGKFIESR TSEWIDIHNP ATNEVIGKVP
     KATQEEMLAA LNSCQRAYPS WSETSVLSRQ QVFLRYQQLI KENMAEIAKL ITKEQGKTLP
     DAEGDVFRGL QVVEHTCSIT SLMLGETLPS ITKDMDTFTY RLPLGVCAGI TPFNFPAMIP
     LWMYPMAMVC GNTFLLKPSE RVPGAAMLLA KLLQDSGAPD GTLNIIHGQH DAVNFICDQP
     AIKAISFVGS NQAGEYIYTR GSENGKRVQS NMGAKNHGVV MPDANKENTL NQLVGAAFGA
     AGQRCMALST AVLVGEAKKW LPELVERAKK LKVNAGDQPG SDLGPLVSPQ AKARVCDLVQ
     SGVEEGAKLL LDGRKIQVKG YENGNFVGPT ILGGVKPQMK CYTEEIFGPV LVVLEAETLD
     EAVDIINQNP YGNGTAIFTT NGATARKFTH HVDVGQIGVN VPIPVPLPMF SFTGSRGSFR
     GDTNFYGKQG IQFYTQVKTV TSQWKEEDAT LTSPSVVMPT MGR
//
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