ID   PAND_METNO              Reviewed;         152 AA.
AC   B8IQG9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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}; OrderedLocusNames=Mnod_5641;
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate
CC       to produce beta-alanine. {ECO:0000255|HAMAP-Rule:MF_00446}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-aspartate = beta-alanine + CO2; Xref=Rhea:RHEA:19497,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:57966; EC=4.1.1.11; Evidence={ECO:0000255|HAMAP-
CC         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. {ECO:0000255|HAMAP-
CC       Rule:MF_00446};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-
CC       alanine from L-aspartate: step 1/1. {ECO:0000255|HAMAP-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 beta-
CC       subunit with a hydroxyl group at its C-terminus and an alpha-subunit
CC       with a pyruvoyl group at its N-terminus. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
CC   -!- SIMILARITY: Belongs to the PanD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00446}.
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DR   EMBL; CP001349; ACL60481.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8IQG9; -.
DR   SMR; B8IQG9; -.
DR   STRING; 460265.Mnod_5641; -.
DR   EnsemblBacteria; ACL60481; ACL60481; Mnod_5641.
DR   KEGG; mno:Mnod_5641; -.
DR   eggNOG; COG0853; Bacteria.
DR   HOGENOM; CLU_115305_1_0_5; -.
DR   OMA; HEPKLVF; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000008207; 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   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR00223; panD; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage; Cytoplasm; Decarboxylase; Lyase;
KW   Pantothenate biosynthesis; Pyruvate; Reference proteome; Schiff base;
KW   Zymogen.
FT   CHAIN           1..23
FT                   /note="Aspartate 1-decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT                   /id="PRO_1000192011"
FT   CHAIN           24..152
FT                   /note="Aspartate 1-decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT                   /id="PRO_1000192012"
FT   ACT_SITE        24
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT   ACT_SITE        57
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT   BINDING         72..74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT   MOD_RES         24
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
SQ   SEQUENCE   152 AA;  17128 MW;  C8446A8A10295D3E CRC64;
     MRRIVAGKLH GIYVTDANLN YHGSITLDPD HCEEAGILPM EFVEIWNKNS GARISTYVIL
     GERGSRCCIL NGAAARTCQP GDQIIICNSI YIRESELPDI RPRVLTFDSD NRVLDRLEYI
     VKFDDFGRYR FAIERARSLN HASIAGEPKT VA