ID A0A249T2B1_9BACT Unreviewed; 470 AA.
AC A0A249T2B1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 12.
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:ASZ13977.1};
GN ORFNames=CK934_25000 {ECO:0000313|EMBL:ASZ13977.1};
OS Chitinophaga sp. MD30.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2033437 {ECO:0000313|EMBL:ASZ13977.1, ECO:0000313|Proteomes:UP000217148};
RN [1] {ECO:0000313|EMBL:ASZ13977.1, ECO:0000313|Proteomes:UP000217148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD30 {ECO:0000313|EMBL:ASZ13977.1,
RC ECO:0000313|Proteomes:UP000217148};
RA Wan X., Darris M., Hou S., Donachie S.P.;
RT "Draft genome sequence of a novel Chitinophaga sp., MD30, isolated from a
RT biofilm in an air conditioner condensate pipe.";
RL Submitted (AUG-2017) 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}.
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DR EMBL; CP023254; ASZ13977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249T2B1; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000217148; 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; 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:ASZ13977.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217148}.
FT DOMAIN 13..344
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 410..464
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 470 AA; 51857 MW; 6A17E4F9B4581ADF CRC64;
MNKDCRKEHD FLGEREIANT VYYGIQTLRA IENFHITGIP ISKEPLFIQG LGYVKKAAAL
ANRDCGVLDQ KLADAIIYAS NKLINGEYVD QFPTDMIQGG AGTSVNMNAN EVIANIGLEY
MGYQKGQYDH LHPNNHVNCS QSTNDAYPTA FRIALYNKMQ HFIKALETLQ KAFYHKGQEF
ARVLKMGRTQ LQDAVPMSLG EEFNGFSTTI KEDIQRIKEA QALITEVNMG ATAIGTMINA
PEGYPVKVTQ YLREVTGIPI VLSEDLIEAT SDTGAYVQLS GTLKRCAIKI SKICNDLRLL
SSGPRAGLNE INLPKLQPGS SIMPGKVNPV IPEVVNQTAY YVIGADVTIT MAAEAGQLQL
NVMEPVIAFS LFTMLGYLEN ACYTLQSKCV DGITANEDVC RNLVMNSIGI VTSLNPILGY
EICASVAKEA LQTGKSVHDI VVLERQLITQ EKWDEVYSFE NMINPKFINN
//
