(data stored in ACNUC7421 zone)

SWISSPROT: C6WGH9_ACTMD

ID   C6WGH9_ACTMD            Unreviewed;       156 AA.
AC   C6WGH9;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 63.
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 alpha chain {ECO:0000256|HAMAP-Rule:MF_00446};
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00446};
GN   Name=panD {ECO:0000256|HAMAP-Rule:MF_00446};
GN   OrderedLocusNames=Amir_0326 {ECO:0000313|EMBL:ACU34295.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34295.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34295.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(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:SAAS00683550}.
CC   -!- CATALYTIC ACTIVITY: L-aspartate = beta-alanine + CO(2).
CC       {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00683552}.
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00446};
CC       Note=Binds 1 pyruvoyl group covalently per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00446};
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:SAAS00683554}.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00683537}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446,
CC       ECO:0000256|SAAS:SAAS00683545}.
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}.
CC   -!- SIMILARITY: Belongs to the PanD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00446, ECO:0000256|SAAS:SAAS00683551}.
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DR   EMBL; CP001630; ACU34295.1; -; Genomic_DNA.
DR   RefSeq; WP_012782958.1; NC_013093.1.
DR   STRING; 446462.Amir_0326; -.
DR   EnsemblBacteria; ACU34295; ACU34295; Amir_0326.
DR   KEGG; ami:Amir_0326; -.
DR   eggNOG; ENOG4108Z2X; Bacteria.
DR   eggNOG; COG0853; LUCA.
DR   HOGENOM; HOG000221007; -.
DR   KO; K01579; -.
DR   OMA; LYSKIHR; -.
DR   OrthoDB; POG091H02LC; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006523; P:alanine biosynthetic process; IEA:InterPro.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd06919; Asp_decarbox; 1.
DR   HAMAP; MF_00446; PanD; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom.
DR   InterPro; IPR003190; Asp_decarbox.
DR   PANTHER; PTHR21012; PTHR21012; 1.
DR   Pfam; PF02261; 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; C6WGH9.
DR   SWISS-2DPAGE; C6WGH9.
KW   Autocatalytic cleavage {ECO:0000256|HAMAP-Rule:MF_00446};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00683553};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00683555};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00446, ECO:0000256|SAAS:SAAS00683556,
KW   ECO:0000313|EMBL:ACU34295.1};
KW   Pantothenate biosynthesis {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00683542};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00683549};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00446,
KW   ECO:0000256|SAAS:SAAS00683539};
KW   Zymogen {ECO:0000256|HAMAP-Rule:MF_00446}.
FT   REGION       73     75       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00446}.
FT   ACT_SITE     25     25       Schiff-base intermediate with substrate;
FT                                via pyruvic acid. {ECO:0000256|HAMAP-
FT                                Rule:MF_00446}.
FT   ACT_SITE     58     58       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00446}.
FT   BINDING      57     57       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00446}.
FT   MOD_RES      25     25       Pyruvic acid (Ser). {ECO:0000256|HAMAP-
FT                                Rule:MF_00446}.
SQ   SEQUENCE   156 AA;  16226 MW;  30DA5680ED3DE8E4 CRC64;
     MFRTMLKSKI HRATVTQADL HYVGSVTVDE DLMDAADLLA GEQVAIVDVT NGARLETYVI
     PGERGSGVIG INGAAAHLVH PGDLVILIAY GSMDDAEARA YRPRVVFVDA DNKVVELGSD
     AARAPEGSGL LSGAVTAQAL AETADAAALD ALIQNQ
//

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