ID   MFNA_HALMA              Reviewed;         350 AA.
AC   Q5V1B4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=rrnAC1798;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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; AY596297; AAV46689.1; -; Genomic_DNA.
DR   RefSeq; WP_007188823.1; NZ_CP039138.1.
DR   AlphaFoldDB; Q5V1B4; -.
DR   SMR; Q5V1B4; -.
DR   STRING; 272569.rrnAC1798; -.
DR   EnsemblBacteria; AAV46689; AAV46689; rrnAC1798.
DR   GeneID; 40152742; -.
DR   KEGG; hma:rrnAC1798; -.
DR   PATRIC; fig|272569.17.peg.2470; -.
DR   eggNOG; arCOG00027; Archaea.
DR   HOGENOM; CLU_028929_2_1_2; -.
DR   OMA; DPHKMGL; -.
DR   UniPathway; UPA00241; -.
DR   Proteomes; UP000001169; Chromosome I.
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   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..350
FT                   /note="Probable L-aspartate decarboxylase"
FT                   /id="PRO_0000147020"
FT   MOD_RES         206
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ   SEQUENCE   350 AA;  37666 MW;  63B2A9E21FF87177 CRC64;
     MLQRAEPQDF ERVLSSMCTV PHPSAREAAE RFLATNPGDP GTYETIAGLE REAVEYLGDI
     TGLSDPAGYV ASGGTEANLQ AIRIARNRAD TDDPNVVAPV HAHFSFTKAA DVLGVELRTA
     PAADYRVNMA AMAELVDEDT VCVVGVAGST EYGYVDPIPA IADLAETVDA LCHVDAAWGG
     FYLPFTDHDW HFGHADIDTM TIDPHKVGQA AVPAGGLLAR DRTLLDELAV ETPYLESTDQ
     LTLTGTRSGA GVASAVAAME SLWPAGYRQQ YETSMANADW LADQLSARGH DVVGPELPLV
     AADLSMPMTD ELRDRGWRVS KTGAGEMRVV CMPHVTRSML RSFVADLDWY