ASPA_ECOLI
ID ASPA_ECOLI Reviewed; 478 AA.
AC P0AC38; P04422; P78140; Q2M6G5;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Aspartate ammonia-lyase;
DE Short=Aspartase;
DE EC=4.3.1.1;
GN Name=aspA; OrderedLocusNames=b4139, JW4099;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=W / ATCC 11105 / DSM 1900;
RX PubMed=2987841; DOI=10.1093/nar/13.6.2063;
RA Takagi J.S., Ida N., Tokushige M., Sakamoto H., Shimura Y.;
RT "Cloning and nucleotide sequence of the aspartase gene of Escherichia coli
RT W.";
RL Nucleic Acids Res. 13:2063-2074(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3541901; DOI=10.1042/bj2370547;
RA Woods S.A., Miles J.S., Roberts R.E., Guest J.R.;
RT "Structural and functional relationships between fumarase and aspartase.
RT Nucleotide sequences of the fumarase (fumC) and aspartase (aspA) genes of
RT Escherichia coli K12.";
RL Biochem. J. 237:547-557(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP MUTAGENESIS OF LYS-55; HIS-124 AND LYS-327.
RX PubMed=8119980; DOI=10.1016/s0021-9258(17)37373-8;
RA Saribas A.S., Schindler J.F., Viola R.E.;
RT "Mutagenic investigation of conserved functional amino acids in Escherichia
RT coli L-aspartase.";
RL J. Biol. Chem. 269:6313-6319(1994).
RN [7]
RP MUTAGENESIS OF ASP-10; ARG-15; HIS-26; ARG-29 AND SER-143.
RX PubMed=9230046; DOI=10.1021/bi970452x;
RA Jayasekera M.M., Shi W., Farber G.K., Viola R.E.;
RT "Evaluation of functionally important amino acids in L-aspartate ammonia-
RT lyase from Escherichia coli.";
RL Biochemistry 36:9145-9150(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND SUBUNIT.
RX PubMed=9230045; DOI=10.1021/bi9704515;
RA Shi W., Dunbar J., Jayasekera M.M.K., Viola R.E., Farber G.K.;
RT "The structure of L-aspartate ammonia-lyase from Escherichia coli.";
RL Biochemistry 36:9136-9144(1997).
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:0000269|PubMed:9230045}.
CC -!- INTERACTION:
CC P0AC38; P0A6Y8: dnaK; NbExp=3; IntAct=EBI-544200, EBI-542092;
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC Aspartase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97038.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X02307; CAA26173.1; -; Genomic_DNA.
DR EMBL; X04066; CAA27701.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97038.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77099.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78141.1; -; Genomic_DNA.
DR PIR; A01159; UFECDW.
DR RefSeq; NP_418562.4; NC_000913.3.
DR RefSeq; WP_000069437.1; NZ_STEB01000014.1.
DR PDB; 1JSW; X-ray; 2.70 A; A/B/C/D=1-478.
DR PDBsum; 1JSW; -.
DR AlphaFoldDB; P0AC38; -.
DR SMR; P0AC38; -.
DR BioGRID; 4262692; 19.
DR DIP; DIP-36166N; -.
DR IntAct; P0AC38; 12.
DR STRING; 511145.b4139; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR jPOST; P0AC38; -.
DR PaxDb; P0AC38; -.
DR PRIDE; P0AC38; -.
DR EnsemblBacteria; AAC77099; AAC77099; b4139.
DR EnsemblBacteria; BAE78141; BAE78141; BAE78141.
DR GeneID; 66671949; -.
DR GeneID; 948658; -.
DR KEGG; ecj:JW4099; -.
DR KEGG; eco:b4139; -.
DR PATRIC; fig|1411691.4.peg.2561; -.
DR EchoBASE; EB0093; -.
DR eggNOG; COG1027; Bacteria.
DR HOGENOM; CLU_021594_4_0_6; -.
DR InParanoid; P0AC38; -.
DR OMA; EICENYV; -.
DR PhylomeDB; P0AC38; -.
DR BioCyc; EcoCyc:ASPARTASE-MON; -.
DR BioCyc; MetaCyc:ASPARTASE-MON; -.
DR BRENDA; 4.3.1.1; 2026.
DR SABIO-RK; P0AC38; -.
DR EvolutionaryTrace; P0AC38; -.
DR PRO; PR:P0AC38; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IDA:EcoCyc.
DR GO; GO:0006531; P:aspartate metabolic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome.
FT CHAIN 1..478
FT /note="Aspartate ammonia-lyase"
FT /id="PRO_0000161338"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 143..145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 10
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9230046"
FT MUTAGEN 10
FT /note="D->N: Reduces Kcal by 80%. Increases KM for aspartic
FT acid 3-fold."
FT /evidence="ECO:0000269|PubMed:9230046"
FT MUTAGEN 15
FT /note="R->A: No effect on kcat. Increases KM for aspartic
FT acid 2.5-fold."
FT /evidence="ECO:0000269|PubMed:9230046"
FT MUTAGEN 26
FT /note="H->N: No effect on kcat. Increases KM for aspartic
FT acid 3-fold."
FT /evidence="ECO:0000269|PubMed:9230046"
FT MUTAGEN 29
FT /note="R->A: No effect on kcat. Increases KM for aspartic
FT acid 40-fold."
FT /evidence="ECO:0000269|PubMed:9230046"
FT MUTAGEN 55
FT /note="K->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8119980"
FT MUTAGEN 124
FT /note="H->L: Reduces activity by 30%."
FT /evidence="ECO:0000269|PubMed:8119980"
FT MUTAGEN 143
FT /note="S->G: Reduces kcat by 90%. Increases KM for aspartic
FT acid 4-fold."
FT /evidence="ECO:0000269|PubMed:9230046"
FT MUTAGEN 143
FT /note="S->T: Reduces kcat by 98.5%. Increases KM for
FT aspartic acid 2-fold."
FT /evidence="ECO:0000269|PubMed:9230046"
FT MUTAGEN 327
FT /note="K->R: Reduces activity by 99.7%. Increases KM for
FT aspartic acid 5-fold."
FT /evidence="ECO:0000269|PubMed:8119980"
FT CONFLICT 32
FT /note="E -> V (in Ref. 2; CAA27701)"
FT /evidence="ECO:0000305"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1JSW"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 47..64
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1JSW"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:1JSW"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 144..180
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1JSW"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1JSW"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 200..224
FT /evidence="ECO:0007829|PDB:1JSW"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1JSW"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:1JSW"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 275..302
FT /evidence="ECO:0007829|PDB:1JSW"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 331..355
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 365..389
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 421..432
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 438..445
FT /evidence="ECO:0007829|PDB:1JSW"
FT HELIX 451..454
FT /evidence="ECO:0007829|PDB:1JSW"
SQ SEQUENCE 478 AA; 52356 MW; B6E8432DBF385DEA CRC64;
MSNNIRIEED LLGTREVPAD AYYGVHTLRA IENFYISNNK ISDIPEFVRG MVMVKKAAAM
ANKELQTIPK SVANAIIAAC DEVLNNGKCM DQFPVDVYQG GAGTSVNMNT NEVLANIGLE
LMGHQKGEYQ YLNPNDHVNK CQSTNDAYPT GFRIAVYSSL IKLVDAINQL REGFERKAVE
FQDILKMGRT QLQDAVPMTL GQEFRAFSIL LKEEVKNIQR TAELLLEVNL GATAIGTGLN
TPKEYSPLAV KKLAEVTGFP CVPAEDLIEA TSDCGAYVMV HGALKRLAVK MSKICNDLRL
LSSGPRAGLN EINLPELQAG SSIMPAKVNP VVPEVVNQVC FKVIGNDTTV TMAAEAGQLQ
LNVMEPVIGQ AMFESVHILT NACYNLLEKC INGITANKEV CEGYVYNSIG IVTYLNPFIG
HHNGDIVGKI CAETGKSVRE VVLERGLLTE AELDDIFSVQ NLMHPAYKAK RYTDESEQ
