ID   ASPA_BACSU              Reviewed;         475 AA.
AC   P26899;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   02-SEP-2026, entry version 148.
DE   RecName: Full=Aspartate ammonia-lyase {ECO:0000250|UniProtKB:Q9LCC6};
DE            Short=Aspartase {ECO:0000303|PubMed:1711029};
DE            EC=4.3.1.1 {ECO:0000250|UniProtKB:Q9LCC6};
GN   Name=ansB {ECO:0000303|PubMed:1711029}; OrderedLocusNames=BSU23570;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-22, AND
RP   TRANSCRIPTIONAL REGULATION.
RC   STRAIN=168 / PS832;
RX   PubMed=1711029; DOI=10.1128/jb.173.12.3831-3845.1991;
RA   Sun D., Setlow P.;
RT   "Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans
RT   operon, which codes for L-asparaginase and L-aspartase.";
RL   J. Bacteriol. 173:3831-3845(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 144 AND 182.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: Catalyzes the reversible conversion of L-aspartate to
CC       fumarate and ammonia. {ECO:0000250|UniProtKB:Q9LCC6}.
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:Q9LCC6};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9LCC6}.
CC   -!- INDUCTION: Part of the ans operon, which contains ansA, encoding L-
CC       asparaginase, and ansB (PubMed:1711029). Contains two transcription
CC       start sites, depending on the growth medium (PubMed:1711029).
CC       {ECO:0000269|PubMed:1711029}.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Aspartase subfamily. {ECO:0000305}.
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DR   EMBL; M63264; AAA22244.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12643.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14289.2; -; Genomic_DNA.
DR   PIR; B39440; UFBSD.
DR   RefSeq; NP_390238.2; NC_000964.3.
DR   RefSeq; WP_003230430.1; NC_000964.3.
DR   AlphaFoldDB; P26899; -.
DR   SMR; P26899; -.
DR   FunCoup; P26899; 49.
DR   IntAct; P26899; 2.
DR   STRING; 224308.BSU23570; -.
DR   jPOST; P26899; -.
DR   PaxDb; 224308-BSU23570; -.
DR   EnsemblBacteria; CAB14289; CAB14289; BSU_23570.
DR   GeneID; 938721; -.
DR   KEGG; bsu:BSU23570; -.
DR   PATRIC; fig|224308.179.peg.2569; -.
DR   eggNOG; COG1027; Bacteria.
DR   InParanoid; P26899; -.
DR   OrthoDB; 9802809at2; -.
DR   PhylomeDB; P26899; -.
DR   BioCyc; BSUB:BSU23570-MONOMER; -.
DR   BRENDA; 4.3.1.1; 658.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P26899; -.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008797; F:aspartate ammonia-lyase activity; ISS:UniProtKB.
DR   GO; GO:0006531; P:aspartate metabolic process; IBA:GO_Central.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd01357; Aspartase; 1.
DR   FunFam; 1.10.40.30:FF:000002; Fumarate hydratase class II; 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; 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   NCBIfam; NF008909; PRK12273.1; 1.
DR   NCBIfam; NF011092; PRK14515.1; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Reference proteome.
FT   CHAIN           1..475
FT                   /note="Aspartate ammonia-lyase"
FT                   /id="PRO_0000161336"
FT   REGION          320..329
FT                   /note="SS loop"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LCC6"
FT   ACT_SITE        321
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LCC6"
FT   BINDING         104
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LCC6"
FT   BINDING         143
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LCC6"
FT   BINDING         144
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         190
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LCC6"
FT   BINDING         191
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LCC6"
FT   BINDING         322
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LCC6"
FT   BINDING         327
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LCC6"
FT   CONFLICT        144
FT                   /note="T -> Q (in Ref. 1; AAA22244 and 2; BAA12643)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="D -> H (in Ref. 1; AAA22244 and 2; BAA12643)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   475 AA;  52504 MW;  F3E847DC83A81460 CRC64;
     MLNGQKEYRV EKDFLGEKQI EADVYYGIQT LRASENFPIT GYKIHEEMIN ALAIVKKAAA
     LANMDVKRLY EGIGQAIVQA ADEILEGKWH DQFIVDPIQG GAGTSMNMNA NEVIGNRALE
     IMGHKKGDYI HLSPNTHVNM SQSTNDVFPT AIHISTLKLL EKLLKTMEDM HSVFKQKAQE
     FDSVIKMGRT HLQDAVPIRL GQEFEAYSRV LERDIKRIKQ SRQHLYEVNM GATAVGTGLN
     ADPEYIKQVV KHLADISGLP LVGADHLVDA TQNTDAYTEV SASLKVCMMN MSKIANDLRL
     MASGPRAGLA EISLPARQPG SSIMPGKVNP VMAELINQIA FQVIGNDNTI CLASEAGQLE
     LNVMEPVLVF NLLQSISIMN NGFRSFTDNC LKGIEANEKR MKQYVEKSAG VITAVNPHLG
     YEAAARIARE AIMTGQSVRD LCLQHDVLTE EELDIILNPY EMTKPGIAGK ELLEK
//