ID I3DE14_HAEPH Unreviewed; 483 AA.
AC I3DE14;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
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:EIJ69957.1};
GN ORFNames=HMPREF1050_0722 {ECO:0000313|EMBL:EIJ69957.1};
OS Haemophilus parahaemolyticus HK385.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1095744 {ECO:0000313|EMBL:EIJ69957.1, ECO:0000313|Proteomes:UP000003016};
RN [1] {ECO:0000313|EMBL:EIJ69957.1, ECO:0000313|Proteomes:UP000003016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK385 {ECO:0000313|EMBL:EIJ69957.1,
RC ECO:0000313|Proteomes:UP000003016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2012) 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:EIJ69957.1}.
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DR EMBL; AJSW01000037; EIJ69957.1; -; Genomic_DNA.
DR RefSeq; WP_005706673.1; NZ_UGHI01000002.1.
DR AlphaFoldDB; I3DE14; -.
DR GeneID; 78223807; -.
DR PATRIC; fig|1095744.4.peg.1238; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000003016; 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:EIJ69957.1}.
FT DOMAIN 12..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 483 AA; 52794 MW; 259710A5D81F7A55 CRC64;
MKDVRIEVDL LGEREVPNEA YWGIHTLRAI ENFNISNNTI SDVPEFVRGM VMVKKATALT
NAELGVIPKK IANAIVQACD EMLEKGRCMD QFPSDVYQGG AGTSVNMNTN EVVANLALEM
LGQPKGRYDI VNPMDHVNAS QSTNDAYPTG FRIAVYNSVL KLIEKIHYLQ QGFEAKAVEF
ADVLKMGRTQ LQDAVPMTVG QEFKAFAVLL EEEVKNLKRT AKLLLEVNLG ATAIGTGLNT
PEGYPELAVK NLAKVTNLPC VLSDNLIEAT SDCGAYVMVH GALKRSAVKL SKVCNDLRLL
SSGPRAGLNE INLPELQAGS SIMPAKVNPV VPEVVNQVCF KVIGNDNTIT FAAEAGQLQL
NVMEPVIGQA MFETISLLSN ACVNLRDKCI DGITVNRETC QNYVFNSIGI VTYLNPFIGH
HNGDIVGKIC AQTGKGVREV VLERGLLTEA ELDDILSVEN LMNPTYKAKR FNEEEQSQLS
SRF
//
