(data stored in ACNUC1104 zone)

SWISSPROT: A4F785_SACEN

ID   A4F785_SACEN            Unreviewed;       484 AA.
AC   A4F785;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   SubName: Full=Malate dehydrogenase (Oxaloacetate-decarboxylating) {ECO:0000313|EMBL:CAL99909.1};
DE            EC=1.1.1.38 {ECO:0000313|EMBL:CAL99909.1};
GN   OrderedLocusNames=SACE_0563 {ECO:0000313|EMBL:CAL99909.1};
GN   ORFNames=A8924_0963 {ECO:0000313|EMBL:PFG93712.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99909.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99909.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99909.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93712.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93712.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000106-3};
CC       Note=Divalent metal cations. Prefers magnesium or manganese.
CC       {ECO:0000256|PIRSR:PIRSR000106-3};
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
CC       {ECO:0000256|RuleBase:RU003427}.
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DR   EMBL; AM420293; CAL99909.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93712.1; -; Genomic_DNA.
DR   RefSeq; WP_009945208.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0563; -.
DR   EnsemblBacteria; CAL99909; CAL99909; SACE_0563.
DR   KEGG; sen:SACE_0563; -.
DR   eggNOG; ENOG4105C6K; Bacteria.
DR   eggNOG; COG0281; LUCA.
DR   HOGENOM; HOG000132447; -.
DR   KO; K00027; -.
DR   OMA; FRGMLDA; -.
DR   OrthoDB; 654531at2; -.
DR   BioCyc; SERY405948:SACE_RS02770-MONOMER; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.10380; -; 1.
DR   InterPro; IPR012301; Malic_N_dom.
DR   InterPro; IPR037062; Malic_N_dom_sf.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM01274; malic; 1.
DR   SMART; SM00919; Malic_M; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F785.
DR   SWISS-2DPAGE; A4F785.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000106-3,
KW   ECO:0000256|RuleBase:RU003427};
KW   Oxidoreductase {ECO:0000313|EMBL:CAL99909.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN       92    225       malic. {ECO:0000259|SMART:SM01274}.
FT   DOMAIN      237    459       Malic_M. {ECO:0000259|SMART:SM00919}.
FT   ACT_SITE    113    113       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   ACT_SITE    168    168       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000106-1}.
FT   METAL       210    210       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       211    211       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
FT   METAL       236    236       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR000106-3}.
SQ   SEQUENCE   484 AA;  50461 MW;  16F260EAF90B282F CRC64;
     MPVPGPGYSI TVRVEAPPSA SAAGDLTGSV GRAGGVITAF DVVESHADRI VVDITCNALS
     ADHANDITDG LRELPGVTVR KVSDRTFLVH LGGKIEVNSR VALTNRDDLS RAYTPGVARV
     CTAIAENPED ARRLTIKRNS VAVVTDGSAV LGLGNIGPEA ALPVMEGKAA LFKKFAGVNA
     WPVCLDTQDT EEIIRAVELI APVYGGINLE DIAAPRCFEI ERRLREKLNI PVFHDDQHGT
     AVVVLGALRN ALRVVGKDLA DCRVVVCGVG AAGSAIIRLL QKKGPADVIA VDIDGIVHTG
     RGDSDPNLQS IAANTNAEGR TGTLSDAVAG ADVFIGVSAP NLLNAEEVAT MNSDAIVFAL
     ANPDPEIDPL EAQKHAKVVA TGRSDYPNQI NNVLAFPGVF RGLLDAHAHE ITDDMMIAAS
     NAIADVVDGE RLNASFIVPS VFDSAVAPAV ADAVRKAATA GRTARPAPVG GSSLPWSMAE
     DLEY
//

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