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Database: UniProt
Entry: G7ZE53_AZOL4
LinkDB: G7ZE53_AZOL4
Original site: G7ZE53_AZOL4 
ID   G7ZE53_AZOL4            Unreviewed;       471 AA.
AC   G7ZE53;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Aspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00016146, ECO:0000256|RuleBase:RU362017};
DE            Short=Aspartase {ECO:0000256|RuleBase:RU362017};
DE            EC=4.3.1.1 {ECO:0000256|ARBA:ARBA00012992, ECO:0000256|RuleBase:RU362017};
GN   Name=aspA {ECO:0000313|EMBL:CBS89896.1};
GN   OrderedLocusNames=AZOLI_p30044 {ECO:0000313|EMBL:CBS89896.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p3 {ECO:0000313|EMBL:CBS89896.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS89896.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p3 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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:0000256|ARBA:ARBA00001494,
CC         ECO:0000256|RuleBase:RU362017};
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Aspartase subfamily. {ECO:0000256|ARBA:ARBA00005596,
CC       ECO:0000256|RuleBase:RU362017}.
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DR   EMBL; FQ311871; CBS89896.1; -; Genomic_DNA.
DR   RefSeq; WP_014249343.1; NC_016623.1.
DR   AlphaFoldDB; G7ZE53; -.
DR   KEGG; ali:AZOLI_p30044; -.
DR   HOGENOM; CLU_021594_4_1_5; -.
DR   OrthoDB; 9802809at2; -.
DR   Proteomes; UP000005667; Plasmid AZO_p3.
DR   GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro.
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 {ECO:0000256|RuleBase:RU362017, ECO:0000313|EMBL:CBS89896.1};
KW   Plasmid {ECO:0000313|EMBL:CBS89896.1}.
FT   DOMAIN          14..344
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          410..462
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   471 AA;  50353 MW;  1D07FDC247DFDA2B CRC64;
     MPATTRTEHD LLGDREVPAD AYYGVHTLRA VENFPITGTP ISHYPDLVRA LAEIKMAAAR
     ANHELGLLGA EQAEAIVAAC REIRAGKLHD QFVVDVIQGG AGTSTNMNAN EVIANRALEI
     LGHGRGDYAH LHPNEHVNMG QSTNDVYPTA LKLATYSGIF RLVEAMGHLR AAFQRKADEF
     RDILKMGRTQ LQDAVPMTLG QEFSTYAVML AEDEERLKEA ALLIREINLG ATAIGTGINA
     HPRYAAVACR HLAEISGVPV VTAPNLVEAT QDCGSFVQLS GVLKRVAVKL SKTCNDLRLL
     SSGPRAGFGE INLPARQAGS SIMPGKVNPV IPEVVNQIAF EVIGNDMTVT FAAEAGQLQL
     NAFEPIIAHS LFKSITHLRQ GCLVLADRCV DGISANREHL EAGVRNSIGI VTALNPYIGY
     ANATEVAAEA HRTGKGVAEL VEARGLMTAA ALAEVLRPEV LTQPRLPATA G
//
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