ID I6DCB3_SHIBO Unreviewed; 478 AA.
AC I6DCB3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:EIQ29405.1};
GN ORFNames=SB444474_4962 {ECO:0000313|EMBL:EIQ29405.1};
OS Shigella boydii 4444-74.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=766140 {ECO:0000313|EMBL:EIQ29405.1, ECO:0000313|Proteomes:UP000004199};
RN [1] {ECO:0000313|EMBL:EIQ29405.1, ECO:0000313|Proteomes:UP000004199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4444-74 {ECO:0000313|EMBL:EIQ29405.1,
RC ECO:0000313|Proteomes:UP000004199};
RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., Jones K.,
RA Santana-Cruz I., Liu X.;
RL Submitted (MAR-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:EIQ29405.1}.
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DR EMBL; AKNB01000305; EIQ29405.1; -; Genomic_DNA.
DR RefSeq; WP_000069437.1; NZ_AKNB01000305.1.
DR AlphaFoldDB; I6DCB3; -.
DR SMR; I6DCB3; -.
DR GeneID; 75203978; -.
DR PATRIC; fig|766140.3.peg.4940; -.
DR Proteomes; UP000004199; 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:EIQ29405.1}.
FT DOMAIN 13..345
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 411..464
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 478 AA; 52356 MW; B6E8432DBF385DEA CRC64;
MSNNIRIEED LLGTREVPAD AYYGVHTLRA IENFYISNNK ISDIPEFVRG MVMVKKAAAM
ANKELQTIPK SVANAIIAAC DEVLNNGKCM DQFPVDVYQG GAGTSVNMNT NEVLANIGLE
LMGHQKGEYQ YLNPNDHVNK CQSTNDAYPT GFRIAVYSSL IKLVDAINQL REGFERKAVE
FQDILKMGRT QLQDAVPMTL GQEFRAFSIL LKEEVKNIQR TAELLLEVNL GATAIGTGLN
TPKEYSPLAV KKLAEVTGFP CVPAEDLIEA TSDCGAYVMV HGALKRLAVK MSKICNDLRL
LSSGPRAGLN EINLPELQAG SSIMPAKVNP VVPEVVNQVC FKVIGNDTTV TMAAEAGQLQ
LNVMEPVIGQ AMFESVHILT NACYNLLEKC INGITANKEV CEGYVYNSIG IVTYLNPFIG
HHNGDIVGKI CAETGKSVRE VVLERGLLTE AELDDIFSVQ NLMHPAYKAK RYTDESEQ
//
