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