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Database: UniProt
Entry: G1VBS5_9BACT
LinkDB: G1VBS5_9BACT
Original site: G1VBS5_9BACT 
ID   G1VBS5_9BACT            Unreviewed;       470 AA.
AC   G1VBS5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
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   ORFNames=HMPREF0666_00858 {ECO:0000313|EMBL:EGW48073.1};
OS   Prevotella sp. C561.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=563031 {ECO:0000313|EMBL:EGW48073.1, ECO:0000313|Proteomes:UP000003086};
RN   [1] {ECO:0000313|EMBL:EGW48073.1, ECO:0000313|Proteomes:UP000003086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C561 {ECO:0000313|EMBL:EGW48073.1,
RC   ECO:0000313|Proteomes:UP000003086};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Sibley C.D., Field T.R.,
RA   Grinwis M., Eshaghurshan C.S., Surette M.G., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. C561.";
RL   Submitted (MAY-2011) 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:EGW48073.1}.
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DR   EMBL; ADCT01000043; EGW48073.1; -; Genomic_DNA.
DR   RefSeq; WP_009011043.1; NZ_JH114141.1.
DR   AlphaFoldDB; G1VBS5; -.
DR   STRING; 563031.HMPREF0666_00858; -.
DR   PATRIC; fig|563031.3.peg.847; -.
DR   eggNOG; COG1027; Bacteria.
DR   HOGENOM; CLU_021594_4_1_10; -.
DR   Proteomes; UP000003086; 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; 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:EGW48073.1}.
FT   DOMAIN          14..345
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          411..463
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   470 AA;  51469 MW;  3F7AD0740A6B0CE9 CRC64;
     MEEKKFRVES DLLGELKVPE EAYYGVQTQR AINNYHISRK RMCDYPDYVV AIAYVKLAAV
     ETNRQLGEIS NEVADAMSEA CREIIDGKMH ENFVTDMVQG GAGTSVNMNA NEVIANRACE
     IMGHKKGEFQ YCSPNDHANC GQSTNDVYPT TIRLTLILLN KKLVASLSEL IAAFRRKGEE
     FKHVIKMGRT QLQDAVPMTS GQEFNAFANT LEEEIANLNR NAALLHEINM GGTAIGTGLN
     AAPGFPKICA EKLSELTGME FIAGVDLVEA TPDTGAYVSY SSALKRLAVK LSKICNDLRL
     LASGPRCGLN EINLPPMAPG SSIMPGKVNP VIPEVTNQTC FKVIGNDTTV MIAAEAGQLQ
     LNVMEPIITE CLIEDLTWLP NAMDTLREKC IDGITVNKDR CLEMVKHSIG IVTALNPYIG
     YKNSTKIAKE ALATGGSVYD LVLEHKLLSK EKLDAILSPE HMLAPEERVK
//
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