ID A0CZZ4_PARTE Unreviewed; 509 AA.
AC A0CZZ4;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
GN ORFNames=GSPATT00011935001 {ECO:0000313|EMBL:CAK76361.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK76361.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK76361.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK76361.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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DR EMBL; CT868230; CAK76361.1; -; Genomic_DNA.
DR RefSeq; XP_001443758.1; XM_001443721.1.
DR AlphaFoldDB; A0CZZ4; -.
DR STRING; 5888.A0CZZ4; -.
DR EnsemblProtists; CAK76361; CAK76361; GSPATT00011935001.
DR GeneID; 5029543; -.
DR KEGG; ptm:GSPATT00011935001; -.
DR eggNOG; KOG2449; Eukaryota.
DR HOGENOM; CLU_005391_1_10_1; -.
DR InParanoid; A0CZZ4; -.
DR OMA; VEYATYV; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IBA:GO_Central.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating, NAD) activity; IBA:GO_Central.
DR GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
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:UP000000600}.
FT DOMAIN 25..488
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 509 AA; 56143 MW; 5F21EB1CA8770B37 CRC64;
MFHNQLRKQS FRFSNIAQNY INGVWKASNG GIALERRSPL TDEVVGITKQ TTQAEFNEAV
DAAKTAFKTW SQVPLPTRQR YMFEYQARIR SKIDDIANII VEEHGKTLAD AKGDVIRGLE
VVEAACGITH VMQGETVENL AKGVDTYSYR VPLGVCAGVC PFNFPAMIPL WMFPIAIVTG
NTYVLKPSER VPGAVTYLTK LLEESGVPKG VVNVVQGGFE TTKHICEHPD IKAVSFVGGN
KAGDYIYENA SKTFKRCQIN MGAKNHGVIM PDADKEDCLN ALASAAFGST GQRCMALSVA
IFVGKSREWI PDLIAKAKSF KVGPGHENID IAPVSYKELY ERIHYLVGTA EKEGGKLILD
GRSFKHPKYP KGYFVGPTII DNMNTNNTSY KEEVFGPVLN ILYADTLDQA LEIINNNPWG
NGTAIFTQNG SIARKFQNEV NAGQIGINLP IPVPLPMFSF TGNKRSFNGD ANFYGKAGIR
FFTQMKTITS RWKEPSDSYT LSTAMPTMK
//
