(data stored in SCRATCH zone)

SWISSPROT: D3VH74_XENNA

ID   D3VH74_XENNA            Unreviewed;       457 AA.
AC   D3VH74;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|SAAS:SAAS00982886};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|SAAS:SAAS00982918};
DE   AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000256|HAMAP-Rule:MF_00006,
GN   ECO:0000313|EMBL:CBJ88359.1};
GN   OrderedLocusNames=XNC1_0271 {ECO:0000313|EMBL:CBJ88359.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88359.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88359.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC         Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:57472; EC=4.3.2.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00006, ECO:0000256|SAAS:SAAS01117070};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 3/3.
CC       {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|SAAS:SAAS00982920}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006,
CC       ECO:0000256|SAAS:SAAS00982890}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00006,
CC       ECO:0000256|SAAS:SAAS00720273}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FN667742; CBJ88359.1; -; Genomic_DNA.
DR   RefSeq; WP_013183208.1; NC_014228.1.
DR   STRING; 406817.XNC1_0271; -.
DR   EnsemblBacteria; CBJ88359; CBJ88359; XNC1_0271.
DR   KEGG; xne:XNC1_0271; -.
DR   eggNOG; ENOG4105CH7; Bacteria.
DR   eggNOG; COG0165; LUCA.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR   CDD; cd01359; Argininosuccinate_lyase; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00006; Arg_succ_lyase; 1.
DR   InterPro; IPR029419; Arg_succ_lyase_C.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
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; PTHR43814; PTHR43814; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00838; argH; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VH74.
DR   SWISS-2DPAGE; D3VH74.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00982884};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00982904};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006,
KW   ECO:0000256|SAAS:SAAS00982916};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|SAAS:SAAS00982881,
KW   ECO:0000313|EMBL:CBJ88359.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN        6    301       Lyase_1. {ECO:0000259|Pfam:PF00206}.
FT   DOMAIN      364    431       ASL_C2. {ECO:0000259|Pfam:PF14698}.
SQ   SEQUENCE   457 AA;  50524 MW;  8157E388793DCB26 CRC64;
     MALWGGRFSQ EADQQFKQFN DSLRFDYRLA EQDIVGSVAW SKALVTVAVL TSEEQQKLEL
     ALNELLDEVR TNPKAILQSD AEDIHSWVEG RLIAKVGDLG KKLHTGRSRN DQVATDLKLW
     CKDQIAHIQQ ALIELQQALV FTAENNQDAV MPGYTHLQRA QPITFAHWCL AYVEMLARDE
     SRLQDALKRL DVSPLGCGAL AGTAYDIDRE QLASWLGFSS ATNNSLDSVS DRDHVLELLS
     GASISMIHLS RFAEDLIFFN SGEAGFIELS DRVTSGSSLM PQKKNPDALE LIRGKCGRVQ
     GSLTGMMMTL KGLPLAYNKD MQEDKEGLFD ALDTWLDCLH MAALVLDGIQ VKQARCEEAA
     KQGYANATEL ADYLVAKGVP FREAHHVVGE VVVDAIAKGK ALEAFSLLEL QKFSDVIAVD
     VYSVLLLKSC LDKRLAKGGV AQEQVQQAVA QAKQRFR
//

If you have problems or comments...

PBIL Back to PBIL home page