ARLY_SYNY3
ID ARLY_SYNY3 Reviewed; 461 AA.
AC P73257;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 148.
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=slr1133;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA17284.1; -; Genomic_DNA.
DR PIR; S77437; S77437.
DR AlphaFoldDB; P73257; -.
DR SMR; P73257; -.
DR IntAct; P73257; 1.
DR STRING; 1148.1652362; -.
DR PaxDb; P73257; -.
DR EnsemblBacteria; BAA17284; BAA17284; BAA17284.
DR KEGG; syn:slr1133; -.
DR eggNOG; COG0165; Bacteria.
DR InParanoid; P73257; -.
DR OMA; KKNPDVF; -.
DR PhylomeDB; P73257; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
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;
KW Reference proteome.
FT CHAIN 1..461
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137841"
SQ SEQUENCE 461 AA; 50948 MW; B6E8C81B1CFB5FE2 CRC64;
MTKKTWSDRF EGTLHPAIAL FNASIGFDIE LIEYDLDGSI AHGKMLAKTG IISPGEAEQL
VQGLEQIRQE YRAGNFNPGV DQEDVHFAVE RRLTELVGDV GKKLHTARSR NDQVGTDVRL
YLRAQIDDIR QRLRDFQAVL LQLAETNVET LIPGYTHLQR AQPVSLAHHL LAYFQMAQRD
WQRLGEIRAR TNVSPLGSGA LAGTTFPIDR HYSAELLGFA GVYANSLDGV SDRDFAIEFL
NAASLIMVHL SRLSEEMILW ASQEFSFISL TDSCATGSSI MPQKKNPDVP ELIRGKAGRV
MGHLQGMLVL MKGLPLAYNK DLQEDKEALF DAVKTVQVSL EAMTILLDEG IVFRQERLAE
AVAEDFSNAT DVADYLAAKG VPFREAYNLV GKVVKTSLAA GKLLKDLTLA EWQALHPAFE
EDIYQAITPQ QVVAARNSYG GTGFEQVKMA IANAKAELSQ T