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Database: UniProt
Entry: V6Q2P7_9ENTE
LinkDB: V6Q2P7_9ENTE
Original site: V6Q2P7_9ENTE 
ID   V6Q2P7_9ENTE            Unreviewed;       458 AA.
AC   V6Q2P7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Adenylosuccinate lyase C-terminal domain-containing protein {ECO:0000259|SMART:SM00998};
GN   ORFNames=T233_01529 {ECO:0000313|EMBL:EST89394.1};
OS   Vagococcus lutrae LBD1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX   NCBI_TaxID=1408226 {ECO:0000313|EMBL:EST89394.1, ECO:0000313|Proteomes:UP000018126};
RN   [1] {ECO:0000313|EMBL:EST89394.1, ECO:0000313|Proteomes:UP000018126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LBD1 {ECO:0000313|EMBL:EST89394.1,
RC   ECO:0000313|Proteomes:UP000018126};
RX   PubMed=24371201;
RA   Lebreton F., Valentino M.D., Duncan L.B., Zeng Q., Manson McGuire A.,
RA   Earl A.M., Gilmore M.S.;
RT   "High-Quality Draft Genome Sequence of Vagococcus lutrae Strain LBD1,
RT   Isolated from the Largemouth Bass Micropterus salmoides.";
RL   Genome Announc. 1:e01087-13(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:EST89394.1}.
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DR   EMBL; AYSH01000019; EST89394.1; -; Genomic_DNA.
DR   RefSeq; WP_023606835.1; NZ_AYSH01000019.1.
DR   AlphaFoldDB; V6Q2P7; -.
DR   STRING; 1408226.T233_01529; -.
DR   GeneID; 72385815; -.
DR   PATRIC; fig|1408226.3.peg.1484; -.
DR   eggNOG; COG0015; Bacteria.
DR   Proteomes; UP000018126; 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:UP000018126}.
FT   DOMAIN          362..441
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
SQ   SEQUENCE   458 AA;  51934 MW;  B06B9DB3EB06FC16 CRC64;
     MRALYDSKSK TMDDRGIKEL FSDKAKYQTW LMFEAALAQA QAEEGFIPEQ AAKDIQQAAK
     IENIDFEEMD RIYREIGHGF VPFLKVLVKA CPPESGKYVH YGITTQNIQQ SSQLYMVKTV
     HDKYMTLLGE ILDNLSRLAE ENKDAVMPGR THGRHATPIT YGYKVSVWIS EFIECYERMR
     EAEKRVFKIM MGGAVGTFSS MPQVGPAVQQ RVAELTGMYT MEVPSRNIST HKLEYMMNLS
     LMANICHKIG EEVYSTTLEE IAEVSEGFKK GTVGSSTMPH KINPKLAKGI VANSQKLYSL
     PGVGMYSSVR PYEGDSSSYM LFDGILEEAL ELTTEVLLRT EELTRTMVPH RDRMLHNALR
     NKGLDNCENV MMVLATKLGK DKAHSLMYEI AMKTANEGED FYTNLMENEL IASQFSEQEV
     RDMIDPRHYI GLSVEIAEKE AKRAKEYANT IALEYANK
//
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