MFNA_NATPD
ID MFNA_NATPD Reviewed; 350 AA.
AC Q3IT46;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
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}; Synonyms=gadD;
GN OrderedLocusNames=NP_1194A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI48688.1; -; Genomic_DNA.
DR RefSeq; WP_011322324.1; NC_007426.1.
DR AlphaFoldDB; Q3IT46; -.
DR SMR; Q3IT46; -.
DR STRING; 348780.NP_1194A; -.
DR EnsemblBacteria; CAI48688; CAI48688; NP_1194A.
DR GeneID; 3702733; -.
DR KEGG; nph:NP_1194A; -.
DR eggNOG; arCOG00027; Archaea.
DR HOGENOM; CLU_028929_2_1_2; -.
DR OMA; DPHKMGL; -.
DR OrthoDB; 44488at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000002698; 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 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_0000293190"
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ SEQUENCE 350 AA; 37765 MW; 76537F9F1D9F5CF9 CRC64;
MQRAEPQEFS RVLSSMCTEP HPAAREAAER FLATNPGDPG TYETVSKLER EAVDMLGEVA
GLPDAAGYIA SGGTEANIQA VRIARNRADT RTPNFVAPAS AHFSFRKAAD ILGVELRTAP
LEDYRANLDG VAELIDSDTA LVVGVAGTTE YGRVDPIPAL ADMAADAGAL CHVDAAWGGF
VLPFTEHAWD FDDADIHTMT IDPHKMGQAA VPAGGLLARG PELLDELAID TPYLESTSQV
TLTGTRSGAG VASAAAVMDE LWRDGYRQQY ETAQTNAHWL AAEVESRGFD VVDPVLPIVA
MDLPYDLVAD LRERGWRLSR TEADEARIVC MPHVTRSMLE EFLTDLDRLA
