ID   E0UU39_SULAO            Unreviewed;       121 AA.
AC   E0UU39;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 82.
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 beta chain {ECO:0000256|HAMAP-Rule:MF_00446};
DE   Contains:
DE     RecName: Full=Aspartate 1-decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00446};
GN   Name=panD {ECO:0000256|HAMAP-Rule:MF_00446};
GN   OrderedLocusNames=Saut_0299 {ECO:0000313|EMBL:ADN08348.1};
OS   Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 /
OS   OK10).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=563040 {ECO:0000313|EMBL:ADN08348.1, ECO:0000313|Proteomes:UP000007803};
RN   [1] {ECO:0000313|EMBL:ADN08348.1, ECO:0000313|Proteomes:UP000007803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC   {ECO:0000313|Proteomes:UP000007803};
RX   PubMed=21304749;
RA   Sikorski J., Munk C., Lapidus A., Ngatchou Djao O.D., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J.F., Tapia R.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Sulfurimonas autotrophica type strain
RT   (OK10).";
RL   Stand. Genomic Sci. 3:194-202(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC   {ECO:0000313|Proteomes:UP000007803};
RX   DOI=10.4056/sigs.1173118;
RA   Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Sims D.,
RA   Meincke L., Brettin T., Detter J., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y., Jeffries C., Rohde M., Lang E., Spring S., Goker M.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA   Klenk H.;
RT   "Complete genome sequence of Sulfurimonas autotrophica type strain
RT   (OK10T).";
RL   Stand. Genomic Sci. 3:194-202(2010).
CC   -!- FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate
CC       to produce beta-alanine. {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00446};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00446, ECO:0000256|PIRSR:PIRSR006246-1};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00446, ECO:0000256|PIRSR:PIRSR006246-1};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-
CC       alanine from L-aspartate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_00446}.
CC   -!- SUBUNIT: Heterooctamer of four alpha and four beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00446}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-
CC       Rule:MF_00446, ECO:0000256|PIRSR:PIRSR006246-3}.
CC   -!- SIMILARITY: Belongs to the PanD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00446}.
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DR   EMBL; CP002205; ADN08348.1; -; Genomic_DNA.
DR   RefSeq; WP_013326104.1; NC_014506.1.
DR   AlphaFoldDB; E0UU39; -.
DR   STRING; 563040.Saut_0299; -.
DR   KEGG; sua:Saut_0299; -.
DR   eggNOG; COG0853; Bacteria.
DR   HOGENOM; CLU_115305_2_0_7; -.
DR   OrthoDB; 9803983at2; -.
DR   UniPathway; UPA00028; UER00002.
DR   Proteomes; UP000007803; 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   Gene3D; 2.40.40.20; -; 1.
DR   HAMAP; MF_00446; PanD; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003190; Asp_decarbox.
DR   NCBIfam; TIGR00223; panD; 1.
DR   PANTHER; PTHR21012; ASPARTATE 1-DECARBOXYLASE; 1.
DR   PANTHER; PTHR21012:SF0; ASPARTATE 1-DECARBOXYLASE; 1.
DR   Pfam; PF02261; Asp_decarbox; 1.
DR   PIRSF; PIRSF006246; Asp_decarbox; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW   Rule:MF_00446};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00446};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00446};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00446};
KW   Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW   ECO:0000256|HAMAP-Rule:MF_00446};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00446};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007803};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_00446};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00446}.
FT   CHAIN           1..24
FT                   /note="Aspartate 1-decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00446,
FT                   ECO:0000256|PIRSR:PIRSR006246-5"
FT                   /id="PRO_5014006603"
FT   CHAIN           25..121
FT                   /note="Aspartate 1-decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00446,
FT                   ECO:0000256|PIRSR:PIRSR006246-5"
FT                   /id="PRO_5014006601"
FT   ACT_SITE        25
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00446,
FT                   ECO:0000256|PIRSR:PIRSR006246-1"
FT   ACT_SITE        58
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00446,
FT                   ECO:0000256|PIRSR:PIRSR006246-1"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00446,
FT                   ECO:0000256|PIRSR:PIRSR006246-2"
FT   BINDING         73..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00446,
FT                   ECO:0000256|PIRSR:PIRSR006246-2"
FT   MOD_RES         25
FT                   /note="Pyruvic acid (Ser)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00446,
FT                   ECO:0000256|PIRSR:PIRSR006246-3"
SQ   SEQUENCE   121 AA;  13780 MW;  CDC69F831D544668 CRC64;
     MTIEMLYSKI HRATVTDANL NYVGSITIDE ELLEASKMRV GQKVEILNIN NGERFSTYII
     LGERGKRDIC LNGAAARKVH KGDKIIVVAY ATYDERELEN YKPRVVLLND ENNIDAIHEE
     I
//