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Database: UniProt
Entry: A4SXN7_POLAQ
LinkDB: A4SXN7_POLAQ
Original site: A4SXN7_POLAQ 
ID   A4SXN7_POLAQ            Unreviewed;       506 AA.
AC   A4SXN7;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE            EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
GN   OrderedLocusNames=Pnuc_1035 {ECO:0000313|EMBL:ABP34251.1};
OS   Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS   QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153 {ECO:0000313|EMBL:ABP34251.1, ECO:0000313|Proteomes:UP000000231};
RN   [1] {ECO:0000313|EMBL:ABP34251.1, ECO:0000313|Proteomes:UP000000231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1
RC   {ECO:0000313|Proteomes:UP000000231};
RX   PubMed=22675600; DOI=10.4056/sigs.2395367;
RA   Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA   Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA   Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT   "Complete genome sequence of Polynucleobacter necessarius subsp.
RT   asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL   Stand. Genomic Sci. 6:74-83(2012).
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DR   EMBL; CP000655; ABP34251.1; -; Genomic_DNA.
DR   RefSeq; WP_011902876.1; NC_009379.1.
DR   AlphaFoldDB; A4SXN7; -.
DR   GeneID; 31481409; -.
DR   KEGG; pnu:Pnuc_1035; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_10_4; -.
DR   Proteomes; UP000000231; Chromosome.
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:SF4; MALONATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABP34251.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000231}.
FT   DOMAIN          28..486
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   506 AA;  54760 MW;  B17928C817E4A241 CRC64;
     MNAPQAYASK DDIGHYVGGS LITPKDGRFS DVYNPSKGTV ARRVALASKQ EVDAAVAVAQ
     KAFETWSLTS PLRRSRILFK YLELLNANRD ELAAIITAEH GKVFTDAQGE VTRGIEIVEF
     ATGIPELLKG DYTEQVSTDI DNWVMRQPLG VVAGITPFNF PVMVPMWMFP MAIACGNTFI
     LKPSPTDPSA SLFMAKLLKE AGLPDGVFNV VQGDKEAVDA LIENPDVKAV SFVGSTPIAN
     YIYERCAHFG KRSQALGGAK NHMVIMPDAD IEKSIDALIG AAYGSAGERC MAISVAVLVG
     DVAEKIMPKL IERTKTLKVK NGMELDAEMG PIVTKAALER ITGYIDSGVA SGAKLLVDGR
     GLKVPGHEDG FFIGGTLFDN VTPDMKIYLE EIFGPVLSCL RVANFTEALN LVNSCEFGNG
     VACFTSDGNI AREFARRVQV GMVGINVPIP VPMAWHGFGG WKKSIFGDMH AYGKEGVRFY
     TKQKSVMQRW PESIAKGAEF VMPTSK
//
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