(data stored in ACNUC7421 zone)

SWISSPROT: C8W637_DESAS

ID   C8W637_DESAS            Unreviewed;       456 AA.
AC   C8W637;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
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   OrderedLocusNames=Dtox_0572 {ECO:0000313|EMBL:ACV61492.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61492.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61492.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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}.
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DR   EMBL; CP001720; ACV61492.1; -; Genomic_DNA.
DR   RefSeq; WP_015756211.1; NC_013216.1.
DR   STRING; 485916.Dtox_0572; -.
DR   EnsemblBacteria; ACV61492; ACV61492; Dtox_0572.
DR   KEGG; dae:Dtox_0572; -.
DR   eggNOG; ENOG4105CH7; Bacteria.
DR   eggNOG; COG0165; LUCA.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   BioCyc; DACE485916:G1GFV-579-MONOMER; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000002217; 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; C8W637.
DR   SWISS-2DPAGE; C8W637.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
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:ACV61492.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN        7    301       Lyase_1. {ECO:0000259|Pfam:PF00206}.
FT   DOMAIN      364    432       ASL_C2. {ECO:0000259|Pfam:PF14698}.
FT   COILED      125    145       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   456 AA;  51234 MW;  ACFEC345D755DE5C CRC64;
     MAKLWGGRFE KESDHLMEDF HSSISFDQRL YKQDIAGSMA HARMLGKAGI ISKAEAERIV
     AGLQEILADI EAGKIEFSVA AEDIHMNIEE LLTQRTGEVG KKLHTARSRN DQVALDVRMY
     LKEEITEVMN LIKYLQDTLA ELAEEHLDTV LPGYTHLQRA QPVTLAHHLM AYYQMFSRDL
     DRLGDCYRRT DVMPLGSGAL AGTTFALDRQ YVAEQLGFAR ISENSLDAVA DRDFAVEFAS
     AASLIMMHLS RFCEEIILWS TAEFAFIELD DAYSTGSSMM PQKKNPDVAE LIRGKTGRVY
     GDLQALLTML KGLPLAYNKD MQEDKEALFD AVDTVKKCLM LFRPMLATVK VKKENMARAA
     RGGFTNATDL ADYLVYKGVP FRQAHEIAGR LVLYCLAKKK TLEEVSLGEY REFSDLIAED
     IYQAIDINHC VEARKVYGGP ARAVVQEAIN RARGKF
//

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