ID A0A2R4X059_9EURY Unreviewed; 349 AA.
AC A0A2R4X059;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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 ECO:0000313|EMBL:AWB27178.1};
GN ORFNames=HARCEL1_05395 {ECO:0000313|EMBL:AWB27178.1};
OS Halococcoides cellulosivorans.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halococcoides.
OX NCBI_TaxID=1679096 {ECO:0000313|EMBL:AWB27178.1, ECO:0000313|Proteomes:UP000244727};
RN [1] {ECO:0000313|EMBL:AWB27178.1, ECO:0000313|Proteomes:UP000244727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HArcel1 {ECO:0000313|EMBL:AWB27178.1,
RC ECO:0000313|Proteomes:UP000244727};
RA Sorokin D.Y., Toshchakov S.V., Samarov N.I., Korzhenkov A., Kublanov I.V.;
RT "Halococcoides cellulosivorans gen. nov., sp. nov., an extremely halophilic
RT cellulose-utilizing haloarchaeon from hypersaline lakes.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP028858; AWB27178.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4X059; -.
DR KEGG; harc:HARCEL1_05395; -.
DR UniPathway; UPA00241; -.
DR Proteomes; UP000244727; 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; 3.90.1150.10; 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:UP000244727}.
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 349 AA; 37496 MW; 7162B6CF553CF70D CRC64;
MLEATPQDFG RVLSSMCTEP CPPARAAADR FLATNPGDPG TYPEIARLEE RAVDLLGEIT
ELADPAGYVA TGGTEANIQA VRIARNRADT DDPVVVAPES AHFSFHKAAA MLDVEIRTTP
LVDYRADPDA IAEAIDSDTA LVVAVAGSTE FGRVDPVPAL AELAHDAGAL CHVDAAWGGF
HLPFTDHDWS FSDAPIDTMT IDPHKAGQAP IPAGGLLARD ESLLEVLEVE TPYLESSTQV
TLTGTRSGAG VAGALAAMET LWPDGYRDNH ERAMANATWL ADELRERGYE VVDPELPLVA
ADVSQSIIDA LRRRGWRISR TGAGDLRIVC MPHVTRSMLR SFVADLDWY
//
