PAND_ALKHC
ID PAND_ALKHC Reviewed; 127 AA.
AC Q9KC85;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=BH1689;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB05408.1; -; Genomic_DNA.
DR PIR; A83861; A83861.
DR RefSeq; WP_010897850.1; NC_002570.2.
DR AlphaFoldDB; Q9KC85; -.
DR SMR; Q9KC85; -.
DR STRING; 272558.10174306; -.
DR EnsemblBacteria; BAB05408; BAB05408; BAB05408.
DR KEGG; bha:BH1689; -.
DR eggNOG; COG0853; Bacteria.
DR HOGENOM; CLU_115305_2_0_9; -.
DR OMA; MLYSKIH; -.
DR OrthoDB; 1751990at2; -.
DR UniPathway; UPA00028; UER00002.
DR Proteomes; UP000001258; 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 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..24
FT /note="Aspartate 1-decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT /id="PRO_0000023027"
FT CHAIN 25..127
FT /note="Aspartate 1-decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT /id="PRO_0000023028"
FT ACT_SITE 25
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT ACT_SITE 58
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT BINDING 73..75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT MOD_RES 25
FT /note="Pyruvic acid (Ser)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
SQ SEQUENCE 127 AA; 13962 MW; 761E66318F893365 CRC64;
MFRTMMKAKL HRARVTESNL NYVGSITIDE DIMDAVDIVE NEKVQIVNNN NGARFETYVI
KGPRGSGVFC LNGAAARLVQ EGDVIIVISY ALVAEENVKE HQPKVAVLNE SNQIVEMLGT
EPASTVL
