ARLY_BACFR
ID ARLY_BACFR Reviewed; 447 AA.
AC Q64Z15;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=BF0512;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD47261.1; -; Genomic_DNA.
DR RefSeq; WP_005784384.1; NZ_UYXF01000019.1.
DR RefSeq; YP_097795.1; NC_006347.1.
DR AlphaFoldDB; Q64Z15; -.
DR SMR; Q64Z15; -.
DR STRING; 295405.BF0512; -.
DR EnsemblBacteria; BAD47261; BAD47261; BF0512.
DR GeneID; 66330440; -.
DR KEGG; bfr:BF0512; -.
DR PATRIC; fig|295405.11.peg.528; -.
DR HOGENOM; CLU_027272_2_0_10; -.
DR OMA; KKNPDVF; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002197; 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.
FT CHAIN 1..447
FT /note="Argininosuccinate lyase"
FT /id="PRO_1000116308"
SQ SEQUENCE 447 AA; 50813 MW; 5634462A32C875DC CRC64;
MAQKLWEKSV EVNKDIERFT VGRDREMDLY LAKHDVLGSM AHITMLESIG LLTKEELAQL
LTELKDIYAS AERGEFVIEE GVEDVHSQVE LMLTRRLGDV GKKIHSGRSR NDQVLLDLKL
FTRTQIREVA EAVEQLFHVL IRQSERYKNV LMPGYTHLQI AMPSSFGLWF GAYAESLVDD
MLFLQAAFKM CNKNPLGSAA GYGSSFPLNR TMTTELLGFD SLNYNVVYAQ MGRGKMERNV
AFALATLAGT ISKLAFDACM FNSQNFGFVK LPDECTTGSS IMPHKKNPDV FELTRAKCNK
LQSLPQQIMM IANNLPSGYF RDLQIIKEVF LPAFQELKDC LQMTTYIMNE IKVNEHILDD
DKYLFIFSVE EVNRLAREGM PFRDAYKKVG LDIEAGHFSH DKQVHHTHEG SIGNLCNDEI
SALMQRTIEG FNFQGMEQAE KTLLGRK
