(data stored in SCRATCH zone)

SWISSPROT: D5USE1_TSUPD

ID   D5USE1_TSUPD            Unreviewed;       135 AA.
AC   D5USE1;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Aspartate 1-decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446};
DE            EC=4.1.1.11 {ECO:0000256|HAMAP-Rule:MF_00446};
DE   AltName: Full=Aspartate alpha-decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446};
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00446};
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00446};
GN   Name=panD {ECO:0000256|HAMAP-Rule:MF_00446};
GN   OrderedLocusNames=Tpau_0568 {ECO:0000313|EMBL:ADG77208.1};
OS   Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS   NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC   Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77208.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA   Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADG77208.1, ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
RX   PubMed=21886861;
RA   Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA   Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA   Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Tsukamurella paurometabola type strain
RT   (no. 33).";
RL   Stand. Genomic Sci. 4:342-351(2011).
CC   -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of
CC       aspartate to produce beta-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_00446, ECO:0000256|SAAS:SAAS00097795}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-aspartate = beta-alanine + CO2;
CC         Xref=Rhea:RHEA:19497, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:57966; EC=4.1.1.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00446,
CC         ECO:0000256|SAAS:SAAS01125291};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00446,
CC         ECO:0000256|PIRSR:PIRSR006246-1};
CC       Note=Binds 1 pyruvoyl group covalently per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|PIRSR:PIRSR006246-
CC       1};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       beta-alanine from L-aspartate: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_00446, ECO:0000256|SAAS:SAAS00097721}.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00097784}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446,
CC       ECO:0000256|SAAS:SAAS00097746}.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme, which is
CC       activated by self-cleavage at a specific serine bond to produce a
CC       beta-subunit with a hydroxyl group at its C-terminus and an alpha-
CC       subunit with a pyruvoyl group at its N-terminus.
CC       {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|PIRSR:PIRSR006246-
CC       3}.
CC   -!- SIMILARITY: Belongs to the PanD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00446, ECO:0000256|SAAS:SAAS01091904}.
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DR   EMBL; CP001966; ADG77208.1; -; Genomic_DNA.
DR   RefSeq; WP_013125250.1; NC_014158.1.
DR   STRING; 521096.Tpau_0568; -.
DR   EnsemblBacteria; ADG77208; ADG77208; Tpau_0568.
DR   KEGG; tpr:Tpau_0568; -.
DR   eggNOG; ENOG4108Z2X; Bacteria.
DR   eggNOG; COG0853; LUCA.
DR   HOGENOM; HOG000221007; -.
DR   KO; K01579; -.
DR   OMA; LYSKIHR; -.
DR   OrthoDB; 1751990at2; -.
DR   BioCyc; TPAU521096:G1GKO-551-MONOMER; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000001213; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006523; P:alanine biosynthetic process; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06919; Asp_decarbox; 1.
DR   HAMAP; MF_00446; PanD; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003190; Asp_decarbox.
DR   PANTHER; PTHR21012; PTHR21012; 1.
DR   Pfam; PF02261; Asp_decarbox; 1.
DR   PIRSF; PIRSF006246; Asp_decarbox; 1.
DR   ProDom; PD009294; Asp_decarbox; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR00223; panD; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5USE1.
DR   SWISS-2DPAGE; D5USE1.
KW   Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_00446};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00097775};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00097760};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00097768,
KW   ECO:0000313|EMBL:ADG77208.1};
KW   Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00097818};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|PIRSR:PIRSR006246-1, ECO:0000256|SAAS:SAAS00097789};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|PIRSR:PIRSR006246-1, ECO:0000256|SAAS:SAAS00097793};
KW   Zymogen {ECO:0000256|HAMAP-Rule:MF_00446}.
FT   CHAIN         1     24       Aspartate 1-decarboxylase beta chain.
FT                                {ECO:0000256|PIRSR:PIRSR006246-5}.
FT                                /FTId=PRO_5014006505.
FT   CHAIN        25    135       Aspartate 1-decarboxylase alpha chain.
FT                                {ECO:0000256|PIRSR:PIRSR006246-5}.
FT                                /FTId=PRO_5014006501.
FT   REGION       73     75       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00446, ECO:0000256|PIRSR:
FT                                PIRSR006246-2}.
FT   ACT_SITE     25     25       Schiff-base intermediate with substrate;
FT                                via pyruvic acid. {ECO:0000256|HAMAP-
FT                                Rule:MF_00446, ECO:0000256|PIRSR:
FT                                PIRSR006246-1}.
FT   ACT_SITE     58     58       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00446, ECO:0000256|PIRSR:PIRSR006246-
FT                                1}.
FT   BINDING      57     57       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00446, ECO:0000256|PIRSR:PIRSR006246-
FT                                2}.
FT   MOD_RES      25     25       Pyruvic acid (Ser). {ECO:0000256|HAMAP-
FT                                Rule:MF_00446, ECO:0000256|PIRSR:
FT                                PIRSR006246-3}.
SQ   SEQUENCE   135 AA;  14266 MW;  E9A99A3FE91BD207 CRC64;
     MLRTMMTSKI HRATVTEANL HYVGSVTVDA DLLDAANLLE GEQVAIVDVT NGARLETYTI
     AGERGSGVIG INGAAAHLVS PGDIVILIAY GQLDERELKT YAPSVVFVDA ENKPVELSTD
     AARVPDGYGL VTGRI
//

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