GenomeNet

Database: UniProt
Entry: ASPA_HAEIN
LinkDB: ASPA_HAEIN
Original site: ASPA_HAEIN 
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   27-MAR-2024, entry version 128.
DE   RecName: Full=Aspartate ammonia-lyase;
DE            Short=Aspartase;
DE            EC=4.3.1.1;
GN   Name=aspA; OrderedLocusNames=HI_0534;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   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   -!- 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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
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   RefSeq; NP_438692.1; NC_000907.1.
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   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   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; Reference proteome.
FT   CHAIN           1..475
FT                   /note="Aspartate ammonia-lyase"
FT                   /id="PRO_0000161341"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145..147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
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
//
DBGET integrated database retrieval system