MFNA_THEKO
ID MFNA_THEKO Reviewed; 384 AA.
AC Q5JJ82;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=L-aspartate decarboxylase {ECO:0000305};
DE Short=ADC {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000305};
DE EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:24415726};
GN Name=mfnA {ECO:0000255|HAMAP-Rule:MF_01610}; OrderedLocusNames=TK1814;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=24415726; DOI=10.1128/jb.01327-13;
RA Tomita H., Yokooji Y., Ishibashi T., Imanaka T., Atomi H.;
RT "An archaeal glutamate decarboxylase homolog functions as an aspartate
RT decarboxylase and is involved in beta-alanine and coenzyme A
RT biosynthesis.";
RL J. Bacteriol. 196:1222-1230(2014).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-aspartate to produce beta-
CC alanine. In vitro, can also catalyzes the decarboxylation of L-
CC glutamate to produce 4-aminobutanoate, but this activity does not seem
CC necessary in vivo. Shows much higher activity with L-aspartate than
CC with L-glutamate. Does not decarboxylate L-tyrosine.
CC {ECO:0000269|PubMed:24415726}.
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, ECO:0000269|PubMed:24415726};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01610,
CC ECO:0000269|PubMed:24415726};
CC -!- ACTIVITY REGULATION: Inhibited by hydroxylamine.
CC {ECO:0000269|PubMed:24415726}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.47 mM for aspartate {ECO:0000269|PubMed:24415726};
CC KM=1.92 mM for glutamate {ECO:0000269|PubMed:24415726};
CC Vmax=1.13 umol/min/mg enzyme with aspartate as substrate
CC {ECO:0000269|PubMed:24415726};
CC Vmax=0.26 umol/min/mg enzyme with glutamate as substrate
CC {ECO:0000269|PubMed:24415726};
CC Note=kcat is 0.80 sec(-1) with aspartate as substrate. kcat is 0.18
CC sec(-1) with glutamate as substrate. {ECO:0000269|PubMed:24415726};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:24415726};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius.
CC {ECO:0000269|PubMed:24415726};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:24415726}.
CC -!- SUBUNIT: Homodimer. Can also form homohexamers.
CC {ECO:0000269|PubMed:24415726}.
CC -!- DISRUPTION PHENOTYPE: No growth on standard medium. Growth can be
CC restored by the addition of exogenous beta-alanine or coenzyme A, but
CC not by the addition of GABA. {ECO:0000269|PubMed:24415726}.
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; AP006878; BAD86003.1; -; Genomic_DNA.
DR RefSeq; WP_011250765.1; NC_006624.1.
DR AlphaFoldDB; Q5JJ82; -.
DR SMR; Q5JJ82; -.
DR STRING; 69014.TK1814; -.
DR EnsemblBacteria; BAD86003; BAD86003; TK1814.
DR GeneID; 3234484; -.
DR KEGG; tko:TK1814; -.
DR PATRIC; fig|69014.16.peg.1770; -.
DR eggNOG; arCOG00027; Archaea.
DR HOGENOM; CLU_028929_2_1_2; -.
DR InParanoid; Q5JJ82; -.
DR OMA; DPHKMGL; -.
DR OrthoDB; 44488at2157; -.
DR PhylomeDB; Q5JJ82; -.
DR BRENDA; 4.1.1.11; 5246.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Decarboxylase; Lyase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..384
FT /note="L-aspartate decarboxylase"
FT /id="PRO_0000147031"
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ SEQUENCE 384 AA; 42545 MW; 3F4F757953FA9C33 CRC64;
MFPERGASEE EVLRELEEKT REDLTFDSGK ILGSMCTYPH PFAVKVVMKY IDRNLGDPGL
HIGSQKIEKE AVDMLANLLG LEKGYGHIVS GGTEANILAV RAMRNLAGIE KPELILPESA
HFSFIKAAEM LGVKLVWAEL NDDYTVNVKD VEKKITDRTI GIVGIAGTTG LGVVDDIPAL
SDLALDYGLP LHVDAAFGGF VIPFAKALGY EIPDFDFRLK GVKSITIDPH KMGMVPIPAG
GIIFREKKFL DSISVLAPYL AGGKIWQATI TGTRPGANAL AVWAMIKHLG FDGYKEVVKE
KMELARWFAS ELKKIPGIYL IREPVLNIVS FGSEKLEELE KELKARGWGV SAHRGYIRIV
VMPHVKREHL EEFLRDLREI AKRL
