ID A0A0Q6A277_9BRAD Unreviewed; 466 AA.
AC A0A0Q6A277;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:KQT20363.1};
DE EC=4.3.1.1 {ECO:0000313|EMBL:KQT20363.1};
GN Name=aspA {ECO:0000313|EMBL:KQT20363.1};
GN ORFNames=ASG57_27950 {ECO:0000313|EMBL:KQT20363.1};
OS Bradyrhizobium sp. Leaf396.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1736363 {ECO:0000313|EMBL:KQT20363.1, ECO:0000313|Proteomes:UP000051536};
RN [1] {ECO:0000313|EMBL:KQT20363.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT20363.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT20363.1, ECO:0000313|Proteomes:UP000051536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf396 {ECO:0000313|EMBL:KQT20363.1,
RC ECO:0000313|Proteomes:UP000051536};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQT20363.1}.
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DR EMBL; LMQJ01000014; KQT20363.1; -; Genomic_DNA.
DR RefSeq; WP_024338992.1; NZ_LMQJ01000014.1.
DR AlphaFoldDB; A0A0Q6A277; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000051536; Unassembled WGS sequence.
DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
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; 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 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 4: Predicted;
KW Lyase {ECO:0000313|EMBL:KQT20363.1}.
FT DOMAIN 11..341
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 407..460
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 466 AA; 50921 MW; 7038BC2C9901CA5C CRC64;
MSRTEQDFLG QREIADDIYY GVQTIRGKEN FHITGIPMNQ EPYFVKALGY VKKAAAMANR
DLGAIDAKVA DAIILGCDRV IAGDMMDQFV TDFIQGGAGT STNMNANEVI ANLALESLGF
AKGDYQHVSP NDHVNYGQST NDTYPTAFRL ALILRLESYM TALRQLQEAF FAKGREFDRV
LKMGRTHLQD AVPMSLGAEF RGWGTTIGEE VERISEARAL LREINLGATA IGTSVTAAVG
YPQLAVRHLG ELTGVDFVLA GDLVEATSDT GAYVQLSGVL KRTASKLTKI CNDIRLLASG
PRAGFNEINL PQLQPGSSIM PGKVNPVIPE VVNQTSFLVI GLDTTVTLAA SAGQLQLNVM
EPVISFALFF SIRTMERAVN SLRENCVVGI TANEEHTRNI VLNSLGIVTV LKPLLGYKLC
AEIAREGYRS GKSLHQIVVV ERKLLTQEKW DEMFSFERLI NPDLIG
//
