ID L9XBF8_9EURY Unreviewed; 361 AA.
AC L9XBF8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Probable L-aspartate decarboxylase {ECO:0000256|HAMAP-Rule:MF_01610};
DE Short=ADC {ECO:0000256|HAMAP-Rule:MF_01610};
DE EC=4.1.1.11 {ECO:0000256|HAMAP-Rule:MF_01610};
GN Name=mfnA {ECO:0000256|HAMAP-Rule:MF_01610};
GN ORFNames=C493_05300 {ECO:0000313|EMBL:ELY59040.1};
OS Natronolimnohabitans innermongolicus JCM 12255.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronolimnohabitans.
OX NCBI_TaxID=1227499 {ECO:0000313|EMBL:ELY59040.1, ECO:0000313|Proteomes:UP000011602};
RN [1] {ECO:0000313|EMBL:ELY59040.1, ECO:0000313|Proteomes:UP000011602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 12255 {ECO:0000313|EMBL:ELY59040.1,
RC ECO:0000313|Proteomes:UP000011602};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Catalyzes the decarboxylation of L-aspartate to produce beta-
CC alanine. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01610};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01610, ECO:0000256|PIRSR:PIRSR602129-50};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01610}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. MfnA
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01610}.
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELY59040.1}.
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DR EMBL; AOHZ01000030; ELY59040.1; -; Genomic_DNA.
DR RefSeq; WP_007258363.1; NZ_AOHZ01000030.1.
DR AlphaFoldDB; L9XBF8; -.
DR STRING; 1227499.C493_05300; -.
DR PATRIC; fig|1227499.3.peg.1079; -.
DR eggNOG; arCOG00027; Archaea.
DR OrthoDB; 56891at2157; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000011602; Unassembled WGS sequence.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR03812; tyr_de_CO2_Arch; 1.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_01610};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01610};
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01610,
KW ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000011602}.
FT MOD_RES 205
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01610,
FT ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 361 AA; 38811 MW; 0D6A0894416BEB28 CRC64;
MQIEPQAFDR VLSSMCTEPH PVAREAAERF LATNPGDPGT YPTVSALEDD AIALLGEIAG
LEDPAGYIAS GGTEANIQAV RIARNRAETR TPNVVMPESA HFSFQKAADV LGVELRIVPT
DEQYRADLEA VRASVDSETA LVIGVAGTTE YGRVDPIPEL GEIARSVDAM CHVDAAWGGF
VLPFTDHEWH FGHAAVDTMA IDPHKMGQAA VPAGGLLARS ADLLDELAVD TPYLESTSQA
TLTGTRSGAG VASAVAAMEE LWPDGYRRQY VRSQNNAEWL ADALEKRGYE VADPTLPLVA
ADVPRSTFDA LRAKGWRISR TATGELRVVC MPHVTREMLA SFIGDLDRLE VRASVPVMSD
D
//
