(data stored in ACNUC7421 zone)

SWISSPROT: ARLY_RHOOB

ID   ARLY_RHOOB              Reviewed;         472 AA.
AC   C1ASZ5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE   AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000255|HAMAP-Rule:MF_00006};
GN   OrderedLocusNames=ROP_06800;
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate +
CC       L-arginine. {ECO:0000255|HAMAP-Rule:MF_00006}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC       arginine from L-ornithine and carbamoyl phosphate: step 3/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
DR   EMBL; AP011115; BAH48927.1; -; Genomic_DNA.
DR   RefSeq; WP_012687930.1; NC_012522.1.
DR   ProteinModelPortal; C1ASZ5; -.
DR   SMR; C1ASZ5; -.
DR   STRING; 632772.ROP_06800; -.
DR   EnsemblBacteria; BAH48927; BAH48927; ROP_06800.
DR   KEGG; rop:ROP_06800; -.
DR   PATRIC; fig|632772.20.peg.741; -.
DR   eggNOG; ENOG4105CH7; Bacteria.
DR   eggNOG; COG0165; LUCA.
DR   HOGENOM; HOG000242744; -.
DR   KO; K01755; -.
DR   OMA; SIMPHKK; -.
DR   OrthoDB; POG091H026A; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
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:SF1; PTHR43814:SF1; 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; C1ASZ5.
DR   SWISS-2DPAGE; C1ASZ5.
KW   Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome;
KW   Cytoplasm; Lyase.
FT   CHAIN         1    472       Argininosuccinate lyase.
FT                                /FTId=PRO_1000116341.
SQ   SEQUENCE   472 AA;  50099 MW;  ED5FF9391A78639B CRC64;
     MSAHGTNEGA LWGGRFESGP AAAMAALSKS THFDWVLAPY DVRASQAHAR VLHKAGLLGD
     EDLATMLDGL GRLAADVASG DFIPSESDED VHGALERGLI DRVGPDVGGR LRAGRSRNDQ
     VATLFRMWLR DAVRRVAEGV LDIVDALATQ AAAHPSAVMP GKTHLQAAQP VLLAHHLLAH
     THPLLRDVQR LRDFDVRAAV SPYGSGALAG SSLGLDPEAI AAELAFDSSA ENSIDATSSR
     DFAAEAAFVL AMIGVDLSRM AEEVILWSTP EFGYITLADA WSTGSSIMPQ KKNPDVSELT
     RGKSGRLIGN LTGLLATLKA QPLAYNRDLQ EDKEPVFDSV AQLELLLPAI TGLVATLEFH
     TDRMAELAPA GFTLATDIAE WLVRQGVPFR VAHEAAGACV RVAEARGAGL EDLTDEELAG
     VDPALTPDVR EVLTVEGSIA SRNARGGTAG IRVAEQLGGV RQLSESLREW CR
//

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