GenomeNet

Database: UniProt
Entry: E4MRR7_CAPOC
LinkDB: E4MRR7_CAPOC
Original site: E4MRR7_CAPOC 
ID   E4MRR7_CAPOC            Unreviewed;       463 AA.
AC   E4MRR7;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
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:EFS97605.1};
GN   ORFNames=HMPREF1977_1077 {ECO:0000313|EMBL:EFS97605.1};
OS   Capnocytophaga ochracea F0287.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=873517 {ECO:0000313|EMBL:EFS97605.1, ECO:0000313|Proteomes:UP000005391};
RN   [1] {ECO:0000313|EMBL:EFS97605.1, ECO:0000313|Proteomes:UP000005391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0287 {ECO:0000313|EMBL:EFS97605.1,
RC   ECO:0000313|Proteomes:UP000005391};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (OCT-2010) 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:EFS97605.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AEOH01000032; EFS97605.1; -; Genomic_DNA.
DR   RefSeq; WP_002673069.1; NZ_GL573160.1.
DR   AlphaFoldDB; E4MRR7; -.
DR   eggNOG; COG1027; Bacteria.
DR   HOGENOM; CLU_021594_4_0_10; -.
DR   Proteomes; UP000005391; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Lyase {ECO:0000256|RuleBase:RU362017, ECO:0000313|EMBL:EFS97605.1}.
FT   DOMAIN          12..343
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          409..461
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
FT   COILED          199..226
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   463 AA;  50394 MW;  7154B1FC85BA8D1C CRC64;
     MTKFRTESDL IGDLQVPADA YYGVQTQRAI ENFRITGTKM GDYPEFVKAI GYVKLAAAQT
     NHALGLLPDE LLKPISEACK EVIEGKFNHQ FLVDMIQGGA GTSVNMNANE VIANRALEIM
     GYEKGDYLHC SPNDHINQSQ STNDAYPTTV KLAAIKMNQT LIKRLALLIE AFRQKGKEFA
     DVIKMGRTQL QDAVPMTLGQ EFEAFAANLE EEIARLQSNA KLFLEINMGG TAIGTGLNAP
     KGYAKLCAEN LAKLTGEAFV TASNLVEATP DTGSYVIYSS ALKRMAVKLS KICNDLRLLS
     SGPRAGLNEI NLPAMQPGSS IMPGKVNPVI PEVVNQVCFK VIGNDLTVTF AAEAGQLQLN
     VMEPVLCQCI IESIVFLERA IDTLRTKCIE GITANREVCL NMVKHSIGIV TALNPHIGYK
     NSTKIAKEAL ETGKSVYNLV LEHGLLSKDK LDEILDPKNM LGV
//
DBGET integrated database retrieval system