ID S0KFX4_9ENTE Unreviewed; 460 AA.
AC S0KFX4;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Adenylosuccinate lyase C-terminal domain-containing protein {ECO:0000259|SMART:SM00998};
GN ORFNames=OMK_02162 {ECO:0000313|EMBL:EOT39825.1};
OS Enterococcus dispar ATCC 51266.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1139219 {ECO:0000313|EMBL:EOT39825.1, ECO:0000313|Proteomes:UP000014127};
RN [1] {ECO:0000313|EMBL:EOT39825.1, ECO:0000313|Proteomes:UP000014127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51266 {ECO:0000313|EMBL:EOT39825.1,
RC ECO:0000313|Proteomes:UP000014127};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus dispar ATCC_51266 (Illumina only
RT assembly).";
RL Submitted (MAR-2013) 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:EOT39825.1}.
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DR EMBL; AHYR01000010; EOT39825.1; -; Genomic_DNA.
DR RefSeq; WP_016173300.1; NZ_KE136354.1.
DR AlphaFoldDB; S0KFX4; -.
DR STRING; 44009.RV01_GL000443; -.
DR PATRIC; fig|1139219.3.peg.2110; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_030949_0_0_9; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000014127; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd01597; pCLME; 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; IPR019468; AdenyloSucc_lyase_C.
DR InterPro; IPR024083; Fumarase/histidase_N.
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; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF10397; ADSL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000014127}.
FT DOMAIN 362..441
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 460 AA; 51303 MW; BCB2FE84E43A6539 CRC64;
MGALYDSKSK TLDDKGIKNL LSPDAKYQAW LTVEAALAKA QGELGVIPVA AATHINEKAQ
IENLDFVKME EIYRKVGHGF VPFLKVFVAA CDEESGKYIH FGATTQNIQQ TSQNLIAKQI
HQKFKQFMLE IMENLANLAK DNAETIMAGR THGKHAIPIT YGYKAAVWLS ELMTSYERLE
EVEKRIFTTM MGGAIGAFNA AGEKGIAVQT RVAKILQMPA MAIPSRNINA PKIEYINVLA
LLANNLHKIA EEVFQTSIEE FGEVSEGFTK GTIGSSTMPH KINPKLSKGI IANAQKLYSL
TSVGYYSAAR PFEADSTTNM LFDGIFTEAL ELMTEILMRG EELTRTLEIH RERMYQNANI
NHGLDNSEFI MMKLAAEIGK DQAHELVYEL AIETELSQKN YADVLLHNEK IQQVFQKKEI
EELLKPENYI GLSVQLAYDT AEAAYELVAK AQKQGDEVHV
//
