MFNA_PYRHO
ID MFNA_PYRHO Reviewed; 383 AA.
AC O58679;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=L-aspartate/L-glutamate decarboxylase {ECO:0000305};
DE Short=ADC/GAD {ECO:0000305};
DE EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:19129626};
DE EC=4.1.1.15 {ECO:0000269|PubMed:19129626};
DE AltName: Full=PhGAD {ECO:0000303|PubMed:19129626};
GN Name=mfnA {ECO:0000255|HAMAP-Rule:MF_01610}; OrderedLocusNames=PH0937;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=19129626; DOI=10.1271/bbb.80583;
RA Kim H.W., Kashima Y., Ishikawa K., Yamano N.;
RT "Purification and characterization of the first archaeal glutamate
RT decarboxylase from Pyrococcus horikoshii.";
RL Biosci. Biotechnol. Biochem. 73:224-227(2009).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-aspartate to produce beta-
CC alanine, and the decarboxylation of L-glutamate to produce 4-
CC aminobutanoate. Can also use cysteate and, to a lesser extent, cysteine
CC sulfite (3-sulfino-L-alanine), but not L-tyrosine. Specific activities
CC toward L-aspartate and cysteate are higher than toward L-glutamate.
CC {ECO:0000269|PubMed:19129626}.
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:19129626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC Evidence={ECO:0000269|PubMed:19129626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-cysteate = CO2 + taurine; Xref=Rhea:RHEA:25221,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58090,
CC ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:19129626};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-sulfino-L-alanine + H(+) = CO2 + hypotaurine;
CC Xref=Rhea:RHEA:16877, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:57853, ChEBI:CHEBI:61085;
CC Evidence={ECO:0000269|PubMed:19129626};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01610,
CC ECO:0000269|PubMed:19129626};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for L-aspartate {ECO:0000269|PubMed:19129626};
CC KM=3.9 mM for L-glutamate {ECO:0000269|PubMed:19129626};
CC KM=2.2 mM for cysteate {ECO:0000269|PubMed:19129626};
CC KM=32.6 mM for cysteine sulfite {ECO:0000269|PubMed:19129626};
CC Note=kcat is 0.34 sec(-1) with L-aspartate as substrate. kcat is 0.26
CC sec(-1) with L-glutamate as substrate. kcat is 0.65 sec(-1) with
CC cysteate as substrate. kcat is 0.03 sec(-1) with cysteine sulfite as
CC substrate. {ECO:0000269|PubMed:19129626};
CC pH dependence:
CC Optimum pH is 8.0 with glutamate as substrate.
CC {ECO:0000269|PubMed:19129626};
CC Temperature dependence:
CC Optimum temperature is higher than 97 degrees Celsius with glutamate
CC as substrate. {ECO:0000269|PubMed:19129626};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01610}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19129626}.
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; BA000001; BAA30034.1; -; Genomic_DNA.
DR PIR; D71084; D71084.
DR RefSeq; WP_010885027.1; NC_000961.1.
DR AlphaFoldDB; O58679; -.
DR SMR; O58679; -.
DR STRING; 70601.3257351; -.
DR EnsemblBacteria; BAA30034; BAA30034; BAA30034.
DR GeneID; 1443262; -.
DR KEGG; pho:PH0937; -.
DR eggNOG; arCOG00027; Archaea.
DR OMA; DPHKMGL; -.
DR OrthoDB; 44488at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004782; F:sulfinoalanine decarboxylase activity; IEA:RHEA.
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 1: Evidence at protein level;
KW Decarboxylase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..383
FT /note="L-aspartate/L-glutamate decarboxylase"
FT /id="PRO_0000147030"
FT MOD_RES 232
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01610"
SQ SEQUENCE 383 AA; 42694 MW; 4954796EEE819044 CRC64;
MKFPRIGLPK EKVIELINEK TKKDLTFSSG KILGSMCTMP HDLAIEVYTK YIDRNLGDPG
LHPGTRKIEE EVIEMISDLL HLEKGHGHIV SGGTEANILA VRAFRNLSDV EKPELILPKS
AHFSFIKAGE MLGVKLVWAE LNPDYTVDVR DVEAKISDNT IGIVGIAGTT GLGVVDDIPA
LSDLARDYGI PLHVDAAFGG FVIPFAKELG YELPDFDFKL KGVQSITIDP HKMGMAPIPA
GGIVFRRKKY LKAISVLAPY LAGGKVWQAT ITGTRPGASV IAVWALIKHL GFEGYMRIVE
RAMKLSRWFA EEIKKINNAW LVREPMLNIV SFQTKNLKKV ERELKSRGWG ISAHRGYIRI
VFMPHVTREM IEEFLKDLKE VLS
