ID F6EKX1_HOYSD Unreviewed; 484 AA.
AC F6EKX1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Aspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00016146, ECO:0000256|RuleBase:RU362017};
DE Short=Aspartase {ECO:0000256|RuleBase:RU362017};
DE EC=4.3.1.1 {ECO:0000256|ARBA:ARBA00012992, ECO:0000256|RuleBase:RU362017};
GN Name=aspA {ECO:0000313|EMBL:AEF41451.1};
GN OrderedLocusNames=AS9A_3004 {ECO:0000313|EMBL:AEF41451.1};
OS Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS (Amycolicicoccus subflavus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC Hoyosella.
OX NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF41451.1, ECO:0000313|Proteomes:UP000009235};
RN [1] {ECO:0000313|EMBL:AEF41451.1, ECO:0000313|Proteomes:UP000009235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX PubMed=21725023; DOI=10.1128/JB.05388-11;
RA Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA Wu X.L.;
RT "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT actinomycete isolated from crude oil-polluted soil.";
RL J. Bacteriol. 193:4538-4539(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate = fumarate + NH4(+); Xref=Rhea:RHEA:16601,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29806, ChEBI:CHEBI:29991; EC=4.3.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001494,
CC ECO:0000256|RuleBase:RU362017};
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC Aspartase subfamily. {ECO:0000256|ARBA:ARBA00005596,
CC ECO:0000256|RuleBase:RU362017}.
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DR EMBL; CP002786; AEF41451.1; -; Genomic_DNA.
DR RefSeq; WP_013807800.1; NC_015564.1.
DR AlphaFoldDB; F6EKX1; -.
DR STRING; 443218.AS9A_3004; -.
DR KEGG; asd:AS9A_3004; -.
DR eggNOG; COG1027; Bacteria.
DR HOGENOM; CLU_021594_4_1_11; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000009235; Chromosome.
DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR CDD; cd01357; Aspartase; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR InterPro; IPR004708; ApsA.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR018951; Fumarase_C_C.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR NCBIfam; TIGR00839; aspA; 1.
DR PANTHER; PTHR42696; ASPARTATE AMMONIA-LYASE; 1.
DR PANTHER; PTHR42696:SF2; ASPARTATE AMMONIA-LYASE; 1.
DR Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU362017, ECO:0000313|EMBL:AEF41451.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT DOMAIN 24..354
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 421..472
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 484 AA; 51843 MW; 83352E6BD3BAF558 CRC64;
MAHMTASSLL ETIGARTETD FMGARKIPAA AYWGIQTLRA VENFSITGTT ISVYPLLIRA
LAQIKHAAVL ANFELGLIDQ TKKDAIQQAC ENIEQGQLLD QFVVDVIQGG AGTSTNMNAN
EVIANRALEI LGLDRGEYST IHPNGDVNMG QSTNDVYPTA IRIATIQGTQ SLLSAMAHLR
RALERKAAEF DDVVKMGRTQ LQDAVPMTLG QEFSTYAVMV DEDERRIREG LVHLHEINLG
ATAIGTGINT HREYAANVCA HLRRITGLPL VTSSNLVEAT QDCGAFVLFS GMLKRVAVKL
SKVCNDLRLL ASGPRAGFAE INLPPRQAGS SIMPGKVNPV IPEVVNQVAF DVIGNDLTIT
MAAEAGQLQL NAFEPIIARS LFASLTSLTS ACTSLADLCI DGITANKEYL RTQVEASIGV
VTVLNPLIGY DAATTIARQA LASGRSVTSL VLESGLLTAH ELDEVLRPER LANPQSDSGE
RALA
//
