(data stored in SCRATCH zone)

SWISSPROT: C3MGM1_SINFN

ID   C3MGM1_SINFN            Unreviewed;       498 AA.
AC   C3MGM1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   SubName: Full=Methylmalonate-semialdehyde dehydrogenase {ECO:0000313|EMBL:ACP24136.1};
DE            EC=1.2.1.27 {ECO:0000313|EMBL:ACP24136.1};
GN   OrderedLocusNames=NGR_c03390 {ECO:0000313|EMBL:ACP24136.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24136.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24136.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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DR   EMBL; CP001389; ACP24136.1; -; Genomic_DNA.
DR   RefSeq; WP_012706921.1; NC_012587.1.
DR   RefSeq; YP_002824889.1; NC_012587.1.
DR   STRING; 394.NGR_c03390; -.
DR   EnsemblBacteria; ACP24136; ACP24136; NGR_c03390.
DR   GeneID; 7791565; -.
DR   KEGG; rhi:NGR_c03390; -.
DR   PATRIC; fig|394.7.peg.3144; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271507; -.
DR   KO; K00140; -.
DR   OMA; LWRETDV; -.
DR   OrthoDB; 490746at2; -.
DR   BioCyc; SFRE394:GBYN-338-MONOMER; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IEA:UniProtKB-EC.
DR   CDD; cd07085; ALDH_F6_MMSDH; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 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   PANTHER; PTHR43866; PTHR43866; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01722; MMSDH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   4: Predicted;
DR   PRODOM; C3MGM1.
DR   SWISS-2DPAGE; C3MGM1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Oxidoreductase {ECO:0000313|EMBL:ACP24136.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN       19    478       Aldedh. {ECO:0000259|Pfam:PF00171}.
FT   ACT_SITE    281    281       {ECO:0000256|PROSITE-ProRule:PRU10008}.
SQ   SEQUENCE   498 AA;  53472 MW;  43ADF727F92A1D2E CRC64;
     MYEVGHFIDG KRVAGKSGRV SNIFNPATGE VQGTVALASD AELAAAVESA KAAQVKWAAT
     NPQRRARVFI KFVQLLNDNM NELAETLSRE HGKTIDDAKG DIVRGLEVCE FVIGIPHLQK
     SEFTEGAGPG IDMYSIRQPV GVGAGITPFN FPGMIPMWMF APAIACGNAF ILKPSERDPS
     VPVRLAELMI EAGLPAGVLN VVNGDKGAVD AILTHPDIAA VSFVGSTPIA RYVYGTAAMN
     GKRAQCFGGA KNHMIIMPDA DLDQAANALI GAGYGSAGER CMAISVAVPV GEETANRLID
     KLTPMVESLR IGPYTDEKAD MGPVVTKEAE QRIRSLIDSG IEQGAKLVVD GRDFKLQGYE
     DGHFIGGCLF DHVTPDMDIY KTEIFGPVLS VVRAKNYEDA LSLPMKHEYG NGVAIYTRDG
     DAARDFASRI NIGMVGVNVP IPVPLAYHSF GGWKSSSFGD LNQHGPDSIK FWTRTKTITE
     RWPSGIKDGA EFSIPTMR
//

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