ID   MFNA_THEGJ              Reviewed;         383 AA.
AC   C5A2X8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Probable L-aspartate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01610};
DE            Short=ADC {ECO:0000255|HAMAP-Rule:MF_01610};
DE            EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_01610};
GN   Name=mfnA {ECO:0000255|HAMAP-Rule:MF_01610}; OrderedLocusNames=TGAM_2137;
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(2007).
CC   -!- FUNCTION: Catalyzes the decarboxylation of L-aspartate to produce beta-
CC       alanine. {ECO:0000255|HAMAP-Rule:MF_01610}.
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_01610};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01610};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01610}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family. MfnA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01610}.
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DR   EMBL; CP001398; ACS34639.1; -; Genomic_DNA.
DR   RefSeq; WP_015859742.1; NC_012804.1.
DR   AlphaFoldDB; C5A2X8; -.
DR   SMR; C5A2X8; -.
DR   STRING; 593117.TGAM_2137; -.
DR   PaxDb; C5A2X8; -.
DR   EnsemblBacteria; ACS34639; ACS34639; TGAM_2137.
DR   GeneID; 7987099; -.
DR   KEGG; tga:TGAM_2137; -.
DR   PATRIC; fig|593117.10.peg.2144; -.
DR   eggNOG; arCOG00027; Archaea.
DR   HOGENOM; CLU_028929_2_1_2; -.
DR   OMA; DPHKMGL; -.
DR   OrthoDB; 44488at2157; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000001488; Chromosome.
DR   GO; GO:0004068; F:aspartate 1-decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01610; MfnA_decarbox; 1.
DR   InterPro; IPR020931; MfnA.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03812; tyr_de_CO2_Arch; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..383
FT                   /note="Probable L-aspartate decarboxylase"
FT                   /id="PRO_1000215704"
FT   MOD_RES         231
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ   SEQUENCE   383 AA;  42646 MW;  364BDD72B54C3056 CRC64;
     MFPERGTDEE EVLEELRRKT REDLTFDSGK ILGSMCTYPH PFAVKIITEF IDRNLGDPGL
     HIGSRKVEEE AVEMLSNLLG LKKGYGHIVS GGTEANILAV RAFRNLAGVE KPELILPKSA
     HFSFIKAGEM LGVKLIWAEL NEDYTVNVRD VEEKITDNTI GIVGIAGTTG LGVVDDIPAL
     SDLALDYGLP LHVDAAFGGF VIPFAKALGY DIPDFDFRLK GVKSITIDPH KMGMVPIPAG
     GIIFRERKYI DAISILAPYL AGGRIWQATI TGTRPGANAL AVWAMIKHLG FEGYKEIVRK
     AMELSQWFAG ELKKIPGVYL IREPVLNIVS FGTENLERVE EELKRRGWGI SAHRGYIRIV
     MMPHVRREHL EEFLRDLEEI VRG