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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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