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Database: UniProt
Entry: C5BYN2_BEUC1
LinkDB: C5BYN2_BEUC1
Original site: C5BYN2_BEUC1 
ID   C5BYN2_BEUC1            Unreviewed;       501 AA.
AC   C5BYN2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=methylmalonate-semialdehyde dehydrogenase (CoA acylating) {ECO:0000256|ARBA:ARBA00013048};
DE            EC=1.2.1.27 {ECO:0000256|ARBA:ARBA00013048};
GN   OrderedLocusNames=Bcav_0729 {ECO:0000313|EMBL:ACQ78990.1};
OS   Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC   Beutenbergia.
OX   NCBI_TaxID=471853 {ECO:0000313|EMBL:ACQ78990.1, ECO:0000313|Proteomes:UP000007962};
RN   [1] {ECO:0000313|EMBL:ACQ78990.1, ECO:0000313|Proteomes:UP000007962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432
RC   {ECO:0000313|Proteomes:UP000007962};
RX   PubMed=21304633; DOI=10.4056/sigs.1162;
RA   Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA   Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT   0122).";
RL   Stand. Genomic Sci. 1:21-28(2009).
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DR   EMBL; CP001618; ACQ78990.1; -; Genomic_DNA.
DR   RefSeq; WP_012725770.1; NC_012669.1.
DR   AlphaFoldDB; C5BYN2; -.
DR   STRING; 471853.Bcav_0729; -.
DR   KEGG; bcv:Bcav_0729; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_005391_1_10_11; -.
DR   OrthoDB; 6882680at2; -.
DR   Proteomes; UP000007962; 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:ACQ78990.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007962}.
FT   DOMAIN          17..477
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   501 AA;  53153 MW;  AFF3E5886E132D69 CRC64;
     MTTIGHWIDG KPYSPAAEKT SPVYDPARGE VVAQLAHATP GEVDEAVGAA SRAFEDWSQV
     SLAKRSSILF GFRELLVAHT DELARIVSRE HGKVISDAKG EIGRGLEVVE FASGIPQLLK
     GEYSPQAATG IDVYSFRQPL GVAVGITPFN FPAMVPLWMA PLAIACGNTF VLKPSERDPS
     ASLFLAQLWA DAGLPDGVFN VVQGDKVAVD ALLTHDDVAA VSFVGSTPIA RYIHATATEH
     GKRVQALGGA KNHAVVLGDA DLDNAAENLT AAAFGAAGER CMAISVAVVE DSVADALVER
     LATKARAVRV RPGSDPDADM GPVITPAAKE RIERLIGSAE DDGATLVVDG RGHVVDGHED
     GFFVGPTVID HVQPEHEAYR EEIFGPVIDV VRVTGLEEAV DVINTNPYGN GTAIFTSSGE
     AARTFQRDVT VGMIGINVPI PVPVAYHSFG GWKDSLFGSS HIYGPEGVAF YTQAKVVTQR
     WPRTRELADR ASFHFSGDST K
//
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