(data stored in SCRATCH zone)

SWISSPROT: C8W3U1_DESAS

ID   C8W3U1_DESAS            Unreviewed;       127 AA.
AC   C8W3U1;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 76.
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=Dtox_0242 {ECO:0000313|EMBL:ACV61195.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61195.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61195.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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; CP001720; ACV61195.1; -; Genomic_DNA.
DR   RefSeq; WP_015755916.1; NC_013216.1.
DR   STRING; 485916.Dtox_0242; -.
DR   EnsemblBacteria; ACV61195; ACV61195; Dtox_0242.
DR   KEGG; dae:Dtox_0242; -.
DR   eggNOG; ENOG4108Z2X; Bacteria.
DR   eggNOG; COG0853; LUCA.
DR   HOGENOM; HOG000221007; -.
DR   KO; K01579; -.
DR   OMA; LYSKIHR; -.
DR   OrthoDB; 1751990at2; -.
DR   BioCyc; DACE485916:G1GFV-247-MONOMER; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000002217; 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; C8W3U1.
DR   SWISS-2DPAGE; C8W3U1.
KW   Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_00446};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
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:ACV61195.1};
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:UP000002217};
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_5013997631.
FT   CHAIN        25    127       Aspartate 1-decarboxylase alpha chain.
FT                                {ECO:0000256|PIRSR:PIRSR006246-5}.
FT                                /FTId=PRO_5013997634.
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   127 AA;  14082 MW;  122EFD70333D7783 CRC64;
     MFLTMFKSKI HRATVTEANL NYMGSITVDR SLLEAANILP HEKVQIVNNN NGNRFETYTI
     AGPRDSGVVC LNGAAARMVQ QGDTVIIIAY TMLDAEEAKT FQPRIVFLDE KNRVERVANG
     ENHGDIG
//

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