ID A0A177HQ77_9ACTN Unreviewed; 470 AA.
AC A0A177HQ77;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
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_2 {ECO:0000313|EMBL:OAH12759.1};
GN ORFNames=STSP_37960 {ECO:0000313|EMBL:OAH12759.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH12759.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH12759.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAH12759.1}.
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DR EMBL; LOHS01000086; OAH12759.1; -; Genomic_DNA.
DR RefSeq; WP_067279190.1; NZ_LOHS01000086.1.
DR AlphaFoldDB; A0A177HQ77; -.
DR STRING; 1716141.STSP_37960; -.
DR PATRIC; fig|1716141.3.peg.3988; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000077381; Unassembled WGS sequence.
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; 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:OAH12759.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077381}.
FT DOMAIN 16..345
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 411..461
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 470 AA; 49771 MW; 91689C790E2A1C90 CRC64;
MTAIAHRSEH DLLGYRDVPA EVYWGIHTLR ARENFPITGM PISAHPYLIE ALAAVKEAAA
RANEELGLLE PRKAAAIIEA CREIRDGKLH DQFVVDVIQG GAGTSTNMNA NEVVANRALE
LLGQARGEYG FLHPNEDVNL GQSTNDVYPT AVKIATVYAV RGLLKAMAVL QDAFAAKAVQ
FRDVLKMGRT QLQDAVPMTL GQEFSAYAVM LEEDRSRLAE AVELIHEINL GATAIGTGLN
APAGYAESAR RHLSQITGLP LVTAVNLVEA TQDCGAFVQM SGVLKRIAVK LSKSCNDLRL
LSSGPRAGLN EINLPPVQAG SSIMPGKVNP VIPEVVNQVA FEVIGNDVTI TMAAEAGQLQ
LNAFEPVILH SLSQSITHLQ RACLTLAERC VAGITANTEA LRAAVENSIG LVTALNPYIG
YEAATGIAKE ALATGRGVAE LVLAKGLLPA GTLAELLRPE VVAGPGQALV
//
