PAND_THET8
ID PAND_THET8 Reviewed; 120 AA.
AC Q5SKN7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=TTHA0606;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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; AP008226; BAD70429.1; -; Genomic_DNA.
DR RefSeq; YP_143872.1; NC_006461.1.
DR PDB; 1VC3; X-ray; 1.50 A; A=1-24, B=26-120.
DR PDB; 2EEO; X-ray; 1.60 A; A=1-24, B=26-120.
DR PDBsum; 1VC3; -.
DR PDBsum; 2EEO; -.
DR AlphaFoldDB; Q5SKN7; -.
DR SMR; Q5SKN7; -.
DR STRING; 300852.55771988; -.
DR EnsemblBacteria; BAD70429; BAD70429; BAD70429.
DR KEGG; ttj:TTHA0606; -.
DR PATRIC; fig|300852.9.peg.604; -.
DR eggNOG; COG0853; Bacteria.
DR HOGENOM; CLU_115305_2_0_0; -.
DR OMA; MLYSKIH; -.
DR PhylomeDB; Q5SKN7; -.
DR UniPathway; UPA00028; UER00002.
DR EvolutionaryTrace; Q5SKN7; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; 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_0000023183"
FT CHAIN 25..120
FT /note="Aspartate 1-decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00446"
FT /id="PRO_0000023184"
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"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:1VC3"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1VC3"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1VC3"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:1VC3"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1VC3"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1VC3"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1VC3"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1VC3"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:1VC3"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1VC3"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:1VC3"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1VC3"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:1VC3"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:1VC3"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1VC3"
SQ SEQUENCE 120 AA; 13095 MW; BAD37D3B6DDD1304 CRC64;
MKRVMFHAKI HRATVTQADL HYVGSVTVDQ DLLDAAGILP FEQVDIYDIT NGARLTTYAL
PGERGSGVIG INGAAAHLVK PGDLVILVAY GVFDEEEARN LKPTVVLVDE RNRILEVRKG
