ID A5FEE7_FLAJ1 Unreviewed; 469 AA.
AC A5FEE7;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=Fjoh_3403 {ECO:0000313|EMBL:ABQ06417.1};
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ06417.1, ECO:0000313|Proteomes:UP000006694};
RN [1] {ECO:0000313|EMBL:ABQ06417.1, ECO:0000313|Proteomes:UP000006694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC UW101 {ECO:0000313|Proteomes:UP000006694};
RX PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
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}.
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DR EMBL; CP000685; ABQ06417.1; -; Genomic_DNA.
DR RefSeq; WP_012025386.1; NZ_MUGZ01000041.1.
DR AlphaFoldDB; A5FEE7; -.
DR STRING; 376686.Fjoh_3403; -.
DR KEGG; fjo:Fjoh_3403; -.
DR eggNOG; COG1027; Bacteria.
DR HOGENOM; CLU_021594_4_1_10; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000006694; Chromosome.
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; 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}.
FT DOMAIN 12..343
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 409..463
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 469 AA; 51400 MW; B021762A9D95C362 CRC64;
MEPTRKEHDF LGELEIPNHL YYGIQTFRAV ENFNITGIPI SKEPLFIKAL GYVKKAAALA
NKDCGAIDSK LAEAICYGSD QVISGKFDKE FVSDLIQGGA GTSVNMNANE VIANIGLEYL
GHKKGEYNFL HPNNHVNCSQ STNDAYPSAF RIALYLKMES FIKTLAGLEV AFAKKGEEFK
EVLKMGRTQL QDAVPMTLGQ EFKAYATTIG EDIQRLKNAQ ELLLEINMGA TAIGTKVNAP
EGYPEICVSY LAKEVGIPLT LSPDLIEATV DTGAYVQIMG TLKRSAVKIS KICNDLRLLS
SGPRTGFNEI NLPARQPGSS IMPGKVNPVI PEVVNQTCFY VIGQDLTVTM AAEAGQLQLN
VMEPVIAFAM FTSLDYLSNA IQTLIDKCIN GITANVDHCY NMVMNSIGIV TQLNPIIGYE
ESASIAGEAL KTNKSVHQIA VVERKLITQE KWDEIYSLEN LIHPKFITK
//
