ID   MFNA_PYRFU              Reviewed;         371 AA.
AC   Q8U1P6;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=PF1159;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009950; AAL81283.1; -; Genomic_DNA.
DR   RefSeq; WP_011012299.1; NC_003413.1.
DR   AlphaFoldDB; Q8U1P6; -.
DR   SMR; Q8U1P6; -.
DR   STRING; 186497.PF1159; -.
DR   EnsemblBacteria; AAL81283; AAL81283; PF1159.
DR   GeneID; 1469028; -.
DR   KEGG; pfu:PF1159; -.
DR   PATRIC; fig|186497.12.peg.1220; -.
DR   eggNOG; arCOG00027; Archaea.
DR   HOGENOM; CLU_028929_2_1_2; -.
DR   OMA; DPHKMGL; -.
DR   PhylomeDB; Q8U1P6; -.
DR   BRENDA; 4.1.1.11; 5243.
DR   BRENDA; 4.1.1.15; 5243.
DR   BRENDA; 4.1.1.25; 5243.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000001013; 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; Reference proteome.
FT   CHAIN           1..371
FT                   /note="Probable L-aspartate decarboxylase"
FT                   /id="PRO_0000147029"
FT   MOD_RES         232
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ   SEQUENCE   371 AA;  40996 MW;  35570E479E145AE5 CRC64;
     MKFPRKGIPQ EEVMRELEKY TSKDLSFSSG KILGSMCTLP HELAKEVFCM YMDRNLGDPG
     LHPGTKKIEE EVIEMLSDLL HLERGYGHIV SGGTEANILA VRAFRNLADV ENPELILPKS
     AHFSFIKAGE MLGVKLIWAD LNPDYTVDVK DVEAKISENT IGIVGIAGTT GLGVVDDIPA
     LSDLARDYGI PLHVDAAFGG FVIPFAKELG YDLPDFDFKL KGVQSITIDP HKMGMAPIPA
     GGIVFRHKKY LRAISVLAPY LAGGKIWQAT ITGTRPGASV LAVWALIKHL GFEGYMEIVD
     RAMKLSRWFA EEIKKTPGAW LVREPMLNIV SFKTKNLRRV ERELKSRGWG ISAHRGYIRI
     VSHASCDGGH D