ARLY1_RHILO
ID ARLY1_RHILO Reviewed; 466 AA.
AC Q98G36;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Argininosuccinate lyase 1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE Short=ASAL 1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase 1 {ECO:0000255|HAMAP-Rule:MF_00006};
GN Name=argH1 {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=mlr3506;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB50380.1; -; Genomic_DNA.
DR RefSeq; WP_010911726.1; NC_002678.2.
DR AlphaFoldDB; Q98G36; -.
DR SMR; Q98G36; -.
DR STRING; 266835.14023775; -.
DR EnsemblBacteria; BAB50380; BAB50380; BAB50380.
DR KEGG; mlo:mlr3506; -.
DR PATRIC; fig|266835.9.peg.2792; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_5; -.
DR OMA; KKNPDVF; -.
DR OrthoDB; 751464at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000000552; 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;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Lyase.
FT CHAIN 1..466
FT /note="Argininosuccinate lyase 1"
FT /id="PRO_0000137810"
SQ SEQUENCE 466 AA; 50778 MW; 7786404E0CFDC557 CRC64;
MSDKKTSNQM WGGRFASGPA AIMEAINASI SFDRKLYAQD IRGSIAHSEM LAQTGIISTA
DQEKIAHGLN TILKEIEAGS FEFSTRLEDI HMNVEARLAD LIGSAAGRLH TARSRNDQVA
VDLRLWVKDE CFRVAEALKG LITALLARAE EHAATVMPGF THMQAAQPVT FGHHCMAYVE
MFARDLSRVR DAIERMDESP LGAAALAGTS FPIDRHRTAK ALGFREPMRN SLDSVSDRDF
ALDFLAMAAI CATHLSRLAE EIIIWSTPQF GFIRLSDSFS TGSSIMPQKK NPDAAELVRG
KTGRVNGHLV GLLTVMKGMP LTYGKDMQED KESVFDAAET LDLMLAAMTG MVSDMTVNAA
AMKKAAGSGH ATATDLADWL VRTLGLPFRE AHHVTGRAVA LAEEKKVSLE KLSLEDLQSI
NPGITADIFS VLAVQNSVKS RTSFGGTAPS EVRKQIRYWK KRLAKA