ID C2M272_CAPGI Unreviewed; 464 AA.
AC C2M272;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
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:EEK15655.1};
GN ORFNames=CAPGI0001_0827 {ECO:0000313|EMBL:EEK15655.1};
OS Capnocytophaga gingivalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=553178 {ECO:0000313|EMBL:EEK15655.1, ECO:0000313|Proteomes:UP000003622};
RN [1] {ECO:0000313|EMBL:EEK15655.1, ECO:0000313|Proteomes:UP000003622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33624 / DSM 3290 / CIP 102945 / JCM 12953 / NCTC 12372 /
RC 27 {ECO:0000313|Proteomes:UP000003622};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) 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:EEK15655.1}.
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DR EMBL; ACLQ01000003; EEK15655.1; -; Genomic_DNA.
DR RefSeq; WP_002665867.1; NZ_ACLQ01000003.1.
DR AlphaFoldDB; C2M272; -.
DR STRING; 553178.CAPGI0001_0827; -.
DR GeneID; 84808557; -.
DR eggNOG; COG1027; Bacteria.
DR Proteomes; UP000003622; 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:EEK15655.1}.
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"
SQ SEQUENCE 464 AA; 50272 MW; 664C52FE0DA32702 CRC64;
MKEFRTESDL LGELQVPKEA YYGVQTQRAL ENFHISTSKM NDYPEFIRAF AFVKLAAAQA
NAALGVIPKE IGAAIEKAAH EIIDGKFHDQ FPVDMFQGGA GTSVNMNTNE VIANRALEIL
GFEKGDYVHC YPNDHVNGSQ STNDSYPTAI KLAVFNMNKI LVKHVQALAD AFRAKGKEFA
DVIKMGRTQL QDAVPMTLGQ EFESYAVSME AEIATLNKTA NSLLEINMGG TAIGTGLNAP
HGYAKLCTEN LAKATGEAFV LSHDLVEATP DTSAYVFYSS ALKKFAVKLS KICNDLRLLA
SGPRAGLSEI NLPPMQPGSS IMPGKVNPVI PEVVNQVCFK VIGNDLTVTF AAEAGQLELN
VMEPVICQAI MESIVLFQNA VDTLKDKCVV GITANREVCL NMVKNSIGIV TALNPHIGYK
NSTKIAKEAL QTGKAVYDLV LDHGLLSKEK LDEILDPKNM IVAK
//
