(data stored in SCRATCH zone)

SWISSPROT: ASPA_BACSU

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   11-DEC-2019, entry version 125.
DE   RecName: Full=Aspartate ammonia-lyase;
DE            Short=Aspartase;
DE            EC=4.3.1.1;
GN   Name=ansB; OrderedLocusNames=BSU23570;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   -!- 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.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Aspartase subfamily. {ECO:0000305}.
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; NZ_JNCM01000036.1.
DR   SMR; P26899; -.
DR   IntAct; P26899; 2.
DR   STRING; 224308.BSU23570; -.
DR   jPOST; P26899; -.
DR   PaxDb; P26899; -.
DR   PRIDE; P26899; -.
DR   EnsemblBacteria; CAB14289; CAB14289; BSU23570.
DR   GeneID; 938721; -.
DR   KEGG; bsu:BSU23570; -.
DR   PATRIC; fig|224308.179.peg.2569; -.
DR   eggNOG; ENOG4108IJ0; Bacteria.
DR   eggNOG; COG1027; LUCA.
DR   HOGENOM; HOG000061737; -.
DR   InParanoid; P26899; -.
DR   KO; K01744; -.
DR   OMA; EICENYV; -.
DR   PhylomeDB; P26899; -.
DR   BioCyc; BSUB:BSU23570-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008797; F:aspartate ammonia-lyase activity; IBA:GO_Central.
DR   GO; GO:0006531; P:aspartate metabolic process; IBA:GO_Central.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IBA:GO_Central.
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;
DR   PRODOM; P26899.
DR   SWISS-2DPAGE; P26899.
KW   Lyase; Reference proteome.
FT   CHAIN           1..475
FT                   /note="Aspartate ammonia-lyase"
FT                   /id="PRO_0000161336"
FT   REGION          143..145
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
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
//

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