ID A0A0B2JSB7_9FIRM Unreviewed; 464 AA.
AC A0A0B2JSB7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:KHM49371.1};
DE EC=4.3.1.1 {ECO:0000313|EMBL:KHM49371.1};
GN Name=aspA {ECO:0000313|EMBL:KHM49371.1};
GN ORFNames=NZ47_12805 {ECO:0000313|EMBL:KHM49371.1};
OS Anaerovibrio lipolyticus.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Anaerovibrio.
OX NCBI_TaxID=82374 {ECO:0000313|EMBL:KHM49371.1, ECO:0000313|Proteomes:UP000030993};
RN [1] {ECO:0000313|EMBL:KHM49371.1, ECO:0000313|Proteomes:UP000030993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5S {ECO:0000313|EMBL:KHM49371.1,
RC ECO:0000313|Proteomes:UP000030993};
RX PubMed=23950883;
RA Prive F., Kaderbhai N.N., Girdwood S., Worgan H.J., Pinloche E.,
RA Scollan N.D., Huws S.A., Newbold C.J.;
RT "Identification and characterization of three novel lipases belonging to
RT families II and V from Anaerovibrio lipolyticus 5ST.";
RL PLoS ONE 8:E69076-E69076(2013).
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:KHM49371.1}.
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DR EMBL; JSCE01000237; KHM49371.1; -; Genomic_DNA.
DR RefSeq; WP_039211712.1; NZ_JSCE01000237.1.
DR AlphaFoldDB; A0A0B2JSB7; -.
DR STRING; 82374.NZ47_12805; -.
DR eggNOG; COG1027; Bacteria.
DR Proteomes; UP000030993; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KHM49371.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030993}.
FT DOMAIN 9..338
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 404..456
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
FT COILED 150..177
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 464 AA; 51033 MW; 3C69832496B5931B CRC64;
MRKEHDFLGE LEVPDDVYYG VQTLRAIENF KITGQRVDSD FVQAMAKVKK ATVLANLSTG
RMPEKIGKAL IQAADEIIEG KLLDQFPVDP IQGGAGTSFN MNMNEVLCNR ALELTGEAKG
RYDIISPNNH GNMAQSTNDT FPTAIKVCLN HKGKNLIKSL NRLVDELEKK GEEYKDIVKM
GRTHLQDAVP ITLGQEMNSY ASSIRRGIER IQHALDTIHY VNMGGTAVGT GLNAEPQYII
NVAKSLSEVT GETYKTADNM IDATNNTDGF ADVSSALKNT ALVIIKMCND FRMMASGPRC
GYYELKLPMR QPGSSIMPGK VNPVIAEVLN QTCYQVIGND LAVTLGVENG QFELNVMEPV
MAFNMFNSIK YLTNAIDGFV DKLLLKLEPN KEQCQMWIDR SVGIVTALLP HVGYENSAMM
AKEAYNTGRP IREVVLEKGL LTKEEIDKIL APAAMTTPGI AGKD
//
