ID A0A2Y9A9U1_9MICO Unreviewed; 505 AA.
AC A0A2Y9A9U1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=SAMN05216184_103222 {ECO:0000313|EMBL:SSA40038.1};
OS Georgenia satyanarayanai.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Georgenia.
OX NCBI_TaxID=860221 {ECO:0000313|EMBL:SSA40038.1, ECO:0000313|Proteomes:UP000250222};
RN [1] {ECO:0000313|EMBL:SSA40038.1, ECO:0000313|Proteomes:UP000250222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10826 {ECO:0000313|EMBL:SSA40038.1,
RC ECO:0000313|Proteomes:UP000250222};
RA Cai Z.;
RL Submitted (OCT-2016) 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; UETB01000003; SSA40038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Y9A9U1; -.
DR Proteomes; UP000250222; 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:SSA40038.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000250222}.
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"
FT REGION 478..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 505 AA; 54513 MW; 869AB9C4226FADAE CRC64;
MAATRTEEDL LGQREIPDDV YWGVHTLRAV ENFSLSGTRV RDLPDLVRGM VLVKKASALT
NRDLRTLPVE IADAIVWACD EMLGTGRCLD QFPVDVYQGG AGTSVNMNVN EVIANLALER
LGLPKGRYDV VHPNDHVNKS QSTNDAYPTG LRIATHQAVE RLKTRLEALA GTFSHKGHEF
SRVLKMGRTQ LQDAVPMTLG QEFSAFAALL TEELLHLSRQ QALLLEVNLG ATAIGTGLNT
PPGYTVRAVA HLAEVTGLPV VRSENLIEAT SDAGAYVSMH AALKRVAVKL DKICNDLRLL
SSGPRAGLGE INLPEMQAGS SIMPAKVNPV IPEVVNQVCF TVIGNDTTVT MAAAAGQLQL
NVMEPVIATA LFESISLLTR ACDTLDRRCV AGITANEEVC RRNVMSSIGL VTFLNPIIGH
HNGDRVGREA ARSGRGVREI VLEWGLLTEA EVDDLLSVEN LMRPRYRGTF YGEDPAVIAP
TADEGRGDED ATEGGELEEG AATDR
//
