ID Q5LQ33_RUEPO Unreviewed; 456 AA.
AC Q5LQ33;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:AAV95908.1};
DE EC=4.3.1.1 {ECO:0000313|EMBL:AAV95908.1};
GN Name=aspA {ECO:0000313|EMBL:AAV95908.1};
GN OrderedLocusNames=SPO2663 {ECO:0000313|EMBL:AAV95908.1};
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV95908.1, ECO:0000313|Proteomes:UP000001023};
RN [1] {ECO:0000313|EMBL:AAV95908.1, ECO:0000313|Proteomes:UP000001023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., Deboy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2] {ECO:0000313|EMBL:AAV95908.1, ECO:0000313|Proteomes:UP000001023}
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC {ECO:0000313|Proteomes:UP000001023};
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
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DR EMBL; CP000031; AAV95908.1; -; Genomic_DNA.
DR RefSeq; WP_011048365.1; NC_003911.12.
DR AlphaFoldDB; Q5LQ33; -.
DR STRING; 246200.SPO2663; -.
DR PaxDb; 246200-SPO2663; -.
DR KEGG; sil:SPO2663; -.
DR eggNOG; COG1027; Bacteria.
DR HOGENOM; CLU_021594_4_1_5; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000001023; Chromosome.
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; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:AAV95908.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT DOMAIN 16..345
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 411..455
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 456 AA; 48124 MW; DBA0559F52030E3B CRC64;
MDTTASRTEH DSIGACTIPQ GAPWGSQTQR AIENFPITGI PISHYPEIVV ALAQVKKACA
LTNAELGALT PDKAAVIASV CDRIIAGQHH EAFCVDVMQG GAGTSTNMNA NEVIANLGLI
VLGGSYGDYG HLHPNDDVNR SQSTNDVYPT AIRLATLSKA RVLSAALRDL VQAFHDKGDE
FAHINKVGRT QLQDAVPMTL GQEFHSFANT LAEDIDRITD LGRLLAEVNL GGTAIGTRIN
TPEGYGPLVV EKLADITGLA LSPARDLIEA SSDLGAFVMF SGALKRVAIK LSKICNDLRL
LSSGPRAGLG EIILPPAQAG SSIMPGKVNP VIPEVVNQIC YQAIGNDLTV TMAAEAGQLQ
LNAMEPVIFY KVMETMTTLT GGMNVLNNRC VRGIRADEKR CAELLGGSLV LATLLAPVIG
YDAAAKVSKR ARAEGITLRE ACLKQGLDAA LVDSLL
//
