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ARLY_PARD8
ID   ARLY_PARD8              Reviewed;         446 AA.
AC   A6LI67;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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}; OrderedLocusNames=BDI_3689;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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:0000255|HAMAP-
CC         Rule:MF_00006};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000255|HAMAP-
CC       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}.
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DR   EMBL; CP000140; ABR45381.1; -; Genomic_DNA.
DR   RefSeq; WP_012056135.1; NZ_LR215978.1.
DR   AlphaFoldDB; A6LI67; -.
DR   SMR; A6LI67; -.
DR   STRING; 435591.BDI_3689; -.
DR   EnsemblBacteria; ABR45381; ABR45381; BDI_3689.
DR   KEGG; pdi:BDI_3689; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_0_10; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   BioCyc; PDIS435591:G1G5A-3784-MON; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000000566; 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; 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; 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;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase;
KW   Reference proteome.
FT   CHAIN           1..446
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000116337"
SQ   SEQUENCE   446 AA;  50368 MW;  418DB936D7700687 CRC64;
     MAQKLWEKNV QVDHEVDIFT VGKDREMDLY LAKYDVLGSM AHITMLESIG LLTKEELNVL
     LAELRNIYAV ADRGEFIIEE GIEDVHSQVE LMLTRRLGDM GKKIHSGRSR NDQVLLDLKL
     FTRSQIQELV ELVSGLFDVL ISQSNRYKDV LLPGYTHLQV AMPSSFGLWF GAYAESLVDD
     LQLMQAAYRI CNRNPLGSAA GYGSSFPLNR QMTTDLLGFD SLDYNVVYAQ MGRGKMERTV
     AFAMAGIAAT LSKLAFDACM FNSQNFGFIK LPDQFTTGSS IMPHKKNPDV FELTRAKCNK
     LQGLPQQIIL ISNNLPSGYF RDLQIIKEVF LPAFDELKDC LRMVTHMMRE VKVNEHILDD
     DKYSLLFSVE EVNRRVLAGM PFRDAYKQVG LDIEAGKFIP SKSVNHTHEG SIGNLCNESI
     TAMMRSVIGS FSFERMNEAE KKLIHG
 
 
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