ID E0SDQ9_DICD3 Unreviewed; 391 AA.
AC E0SDQ9;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Argininosuccinate lyase {ECO:0000313|EMBL:ADN00751.1};
DE EC=4.3.2.1 {ECO:0000313|EMBL:ADN00751.1};
GN OrderedLocusNames=Dda3937_01103 {ECO:0000313|EMBL:ADN00751.1};
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628 {ECO:0000313|EMBL:ADN00751.1, ECO:0000313|Proteomes:UP000006859};
RN [1] {ECO:0000313|EMBL:ADN00751.1, ECO:0000313|Proteomes:UP000006859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937 {ECO:0000313|EMBL:ADN00751.1,
RC ECO:0000313|Proteomes:UP000006859};
RX PubMed=21217001; DOI=10.1128/JB.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
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DR EMBL; CP002038; ADN00751.1; -; Genomic_DNA.
DR RefSeq; WP_013320143.1; NC_014500.1.
DR AlphaFoldDB; E0SDQ9; -.
DR STRING; 198628.Dda3937_01103; -.
DR GeneID; 9736052; -.
DR KEGG; ddd:Dda3937_01103; -.
DR PATRIC; fig|198628.6.peg.4505; -.
DR eggNOG; COG2232; Bacteria.
DR HOGENOM; CLU_705420_0_0_6; -.
DR OrthoDB; 9765608at2; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003806; ATP-grasp_PylC-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF02655; ATP-grasp_3; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000313|EMBL:ADN00751.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000006859}.
FT DOMAIN 111..302
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 391 AA; 43485 MW; B198AA93CC33D48C CRC64;
MEHILFIETR GMNPTGILNA AIARGYHPVI ATVQGDEWRQ RLREQHIEAT LLTVPRLAPQ
DILSALPFRP VAVITLSDQY LEIGADVARQ LDLPHTPVDV LASCRDKQAT RRLVAATTVK
QPAFARIENR ENMHDVVLSE LVGFPLIFKP LLGHSSLGVH KFYAQSDVDD FFRQETDRFD
FPYIVEHLIE DAELISVEGF VDRIGVHFLG CSSRLLGGEG DCVELGGIFP YRPFEALLYQ
ASREIIRAID MSFGAFHIEY LVRDNQVYLV EVNPRFPNGP APSNISRALG GSLDDVIIDL
FVNGFSASRP IPKYVSIARA LYSEQGGTIT NIHVPDDIDA DVFISSSTPF KVNRIRSNAD
RFGFVITASD DVALLDDKVN AIMKQIAIEI G
//
