(data stored in ACNUC7421 zone)

SWISSPROT: PAND_SYNFM

ID   PAND_SYNFM              Reviewed;         124 AA.
AC   A0LF66;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=Aspartate 1-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446};
DE            EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00446};
DE   AltName: Full=Aspartate alpha-decarboxylase {ECO:0000255|HAMAP-Rule:MF_00446};
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00446};
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00446};
DE   Flags: Precursor;
GN   Name=panD {ECO:0000255|HAMAP-Rule:MF_00446};
GN   OrderedLocusNames=Sfum_0368;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of
CC       aspartate to produce beta-alanine. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
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:0000255|HAMAP-Rule:MF_00446};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00446};
CC       Note=Binds 1 pyruvoyl group covalently per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_00446};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis;
CC       beta-alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00446}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00446}.
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:0000255|HAMAP-Rule:MF_00446}.
CC   -!- SIMILARITY: Belongs to the PanD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
DR   EMBL; CP000478; ABK16068.1; -; Genomic_DNA.
DR   RefSeq; WP_011697241.1; NC_008554.1.
DR   SMR; A0LF66; -.
DR   STRING; 335543.Sfum_0368; -.
DR   EnsemblBacteria; ABK16068; ABK16068; Sfum_0368.
DR   KEGG; sfu:Sfum_0368; -.
DR   eggNOG; ENOG4108Z2X; Bacteria.
DR   eggNOG; COG0853; LUCA.
DR   HOGENOM; HOG000221007; -.
DR   KO; K01579; -.
DR   OMA; LYSKIHR; -.
DR   OrthoDB; 1751990at2; -.
DR   BioCyc; SFUM335543:G1G7I-373-MONOMER; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000001784; 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; A0LF66.
DR   SWISS-2DPAGE; A0LF66.
KW   Autocatalytic cleavage; Complete proteome; Cytoplasm; Decarboxylase;
KW   Lyase; Pantothenate biosynthesis; Pyruvate; Reference proteome;
KW   Schiff base; Zymogen.
FT   CHAIN         1     24       Aspartate 1-decarboxylase beta chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_00446}.
FT                                /FTId=PRO_0000307073.
FT   CHAIN        25    124       Aspartate 1-decarboxylase alpha chain.
FT                                {ECO:0000255|HAMAP-Rule:MF_00446}.
FT                                /FTId=PRO_0000307074.
FT   REGION       73     75       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   ACT_SITE     25     25       Schiff-base intermediate with substrate;
FT                                via pyruvic acid. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   ACT_SITE     58     58       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   BINDING      57     57       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
FT   MOD_RES      25     25       Pyruvic acid (Ser). {ECO:0000255|HAMAP-
FT                                Rule:MF_00446}.
SQ   SEQUENCE   124 AA;  13499 MW;  CE75C59519204CB4 CRC64;
     MQRLMLKSKI HRARVTEANL HYEGSLTIDE TLMKAADILP YEQIKVYNVF NGARFDTYAI
     AGPAGSGVFC LNGAAARMGA AGDLIIIATY AQYDEAEIAR HQPKVVLLDG DNRPLSQGLK
     ACLS
//

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