ID ASPA_HAEIN Reviewed; 475 AA. AC P44324; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 04-NOV-2026, entry version 135. DE RecName: Full=Aspartate ammonia-lyase {ECO:0000250|UniProtKB:P0AC38}; DE Short=Aspartase {ECO:0000250|UniProtKB:P0AC38}; DE EC=4.3.1.1 {ECO:0000250|UniProtKB:P0AC38}; GN Name=aspA; OrderedLocusNames=HI_0534; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pasteurellales; Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Catalyzes the reversible conversion of L-aspartate to CC fumarate and ammonia. {ECO:0000250|UniProtKB:P0AC38}. 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:0000250|UniProtKB:P0AC38}; CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AC38}. CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family. CC Aspartase subfamily. {ECO:0000305}. 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; L42023; AAC22191.1; -; Genomic_DNA. DR PIR; C64075; C64075. DR AlphaFoldDB; P44324; -. DR SMR; P44324; -. DR STRING; 71421.HI_0534; -. DR MoonProt; P44324; -. DR EnsemblBacteria; AAC22191; AAC22191; HI_0534. DR KEGG; hin:HI_0534; -. DR PATRIC; fig|71421.8.peg.553; -. DR eggNOG; COG1027; Bacteria. DR HOGENOM; CLU_021594_4_0_6; -. DR OMA; AAAQCMF; -. DR OrthoDB; 9802809at2; -. DR PhylomeDB; P44324; -. DR BioCyc; HINF71421:G1GJ1-547-MONOMER; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IDA:CAFA. DR GO; GO:0006531; P:aspartate metabolic process; IBA:GO_Central. DR GO; GO:0010756; P:positive regulation of plasminogen activation; IDA:CAFA. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR CDD; cd01357; Aspartase; 1. DR FunFam; 1.10.40.30:FF:000003; Aspartate ammonia-lyase; 1. DR FunFam; 1.10.275.10:FF:000001; Fumarate hydratase, mitochondrial; 1. DR FunFam; 1.20.200.10:FF:000001; Fumarate hydratase, mitochondrial; 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; IPR051546; Aspartate_Ammonia-Lyase. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR018951; Fumarase_C_C. DR InterPro; IPR022761; Fumarate-Lyase-like_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR008948; L-Aspartase-like. DR NCBIfam; TIGR00839; aspA; 1. DR NCBIfam; NF008909; PRK12273.1; 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; Reference proteome. FT CHAIN 1..475 FT /note="Aspartate ammonia-lyase" FT /id="PRO_0000161341" FT REGION 322..331 FT /note="SS loop" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT ACT_SITE 323 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 106 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 145 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 146 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 147 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 192 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 324 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" FT BINDING 329 FT /ligand="L-aspartate" FT /ligand_id="ChEBI:CHEBI:29991" FT /evidence="ECO:0000250|UniProtKB:Q9LCC6" SQ SEQUENCE 475 AA; 51483 MW; E89F8041436EB9EA CRC64; MITMTQFRKE VDLLGERDVP AEAYWGIHTL RAVENFNISN VTISDVPEFV RGMVMVKKAT ALANGELGAI PSDIAKAIVA ACDEILTTGK CLDQFPSDVY QGGAGTSVNM NTNEVVANLA LEKIGHKKGE YNVINPMDHV NASQSTNDAY PTGFRIAVYN SILKLIDKIQ YLHDSFDNKA KEFANILKMG RTQLQDAVPM TVGQEFKAFA VLLEEEVRNL KRTAGLLLEV NLGATAIGTG LNTPQGYTEL VVKHLAEVTG LACVPAENLI EATSDCGAYV MVHGALKRTA VKLSKVCNDL RLLSSGPRAG LKEINLPELQ AGSSIMPAKV NPVVPEVVNQ VCFKVIGNDT TVTFASEAGQ LQLNVMEPVI GQAMFESIDI LTNACVNLRD KCVDGITVNK EICENYVFNS IGIVTYLNPF IGHHNGDLVG KICAQTGKGV REVVLEKGLL TEEQLDDILS VENLMNPTYK AKLNK //