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 03-AUG-2022, entry version 123.
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; Proteobacteria; 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}.
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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 OMA; EICENYV; -.
DR PhylomeDB; P44324; -.
DR BioCyc; HINF71421:G1GJ1-547-MON; -.
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 Gene3D; 1.10.275.10; -; 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 Pfam; PF10415; FumaraseC_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00839; aspA; 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