ID   MFNA_HALSA              Reviewed;         355 AA.
AC   Q9HSA3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 105.
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=VNG_0327G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG18904.1; -; Genomic_DNA.
DR   PIR; D84192; D84192.
DR   RefSeq; WP_010902198.1; NC_002607.1.
DR   AlphaFoldDB; Q9HSA3; -.
DR   SMR; Q9HSA3; -.
DR   STRING; 64091.VNG_0327G; -.
DR   PaxDb; Q9HSA3; -.
DR   EnsemblBacteria; AAG18904; AAG18904; VNG_0327G.
DR   GeneID; 5953976; -.
DR   KEGG; hal:VNG_0327G; -.
DR   PATRIC; fig|64091.14.peg.243; -.
DR   HOGENOM; CLU_028929_2_1_2; -.
DR   InParanoid; Q9HSA3; -.
DR   OMA; DPHKMGL; -.
DR   OrthoDB; 44488at2157; -.
DR   PhylomeDB; Q9HSA3; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0004068; F:aspartate 1-decarboxylase activity; IBA:GO_Central.
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; IBA:GO_Central.
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   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR03812; tyr_de_CO2_Arch; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..355
FT                   /note="Probable L-aspartate decarboxylase"
FT                   /id="PRO_0000147021"
FT   MOD_RES         210
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ   SEQUENCE   355 AA;  37357 MW;  97D065DB8491B6A2 CRC64;
     MTRGEARRPP QEFDRVLSSM CTTPHPAARE AAQAFLATNP GDPETYPAVA ERERDAVALL
     GEIVGLSSPH GYIAAGGTEA NLQAVRAARN RADADAVNVV APASAHFSFQ KAADVLGVEL
     RLAPTDGDHR ADVAAVADLV DGDTAVVVGV AGTTEYGRVD PIPALADIAA GVDANLHVDA
     AWGGFVLPFT DHDWSFADAP VNTMAIDPHK MGQAPVPAGG FLARDPETLD ALAIETPYLE
     SDTQPTLGGT RSGAGVAGAL ASLRALWPDG YREQYERTQG NAEYLAAELA ARGYDVVDPE
     LPLVAADMPD AEFQALREEG WRISRTASDA LRVVCMPHVT REMLAAFLDD VDALA