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PAND_THISH
ID   PAND_THISH              Reviewed;         126 AA.
AC   B8GNA7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=Tgr7_0877;
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7;
RX   PubMed=21475584; DOI=10.4056/sigs.1483693;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL71968.1; -; Genomic_DNA.
DR   RefSeq; WP_012637456.1; NC_011901.1.
DR   AlphaFoldDB; B8GNA7; -.
DR   SMR; B8GNA7; -.
DR   STRING; 396588.Tgr7_0877; -.
DR   EnsemblBacteria; ACL71968; ACL71968; Tgr7_0877.
DR   KEGG; tgr:Tgr7_0877; -.
DR   eggNOG; COG0853; Bacteria.
DR   HOGENOM; CLU_115305_2_1_6; -.
DR   OMA; MLYSKIH; -.
DR   OrthoDB; 1751990at2; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000002383; 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_1000135232"
FT   CHAIN           25..126
FT                   /note="Aspartate 1-decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT                   /id="PRO_1000135233"
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   126 AA;  13738 MW;  76D9AA39F7043286 CRC64;
     MLLTLLKCKL HKATVTHSEL EYEGSCAIDG DLLDAAGILP YEQIQIYNIA NGERFTTYAI
     RAEAGSRVIS VNGAAAHKAN PGDRVIICAY GQLPREEAAR FHPRLVYLDA DNRIVRTGSD
     IPVQAA
 
 
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