ARLY_STRT2
ID ARLY_STRT2 Reviewed; 461 AA.
AC Q5M2K3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 106.
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=stu1812;
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311;
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV61411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000023; AAV61411.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002953530.1; NC_006448.1.
DR AlphaFoldDB; Q5M2K3; -.
DR SMR; Q5M2K3; -.
DR STRING; 264199.stu1812; -.
DR EnsemblBacteria; AAV61411; AAV61411; stu1812.
DR GeneID; 66899549; -.
DR KEGG; stl:stu1812; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_9; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001170; 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;
KW Reference proteome.
FT CHAIN 1..461
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000240778"
SQ SEQUENCE 461 AA; 51979 MW; 90738E7AF464C0F3 CRC64;
MAENHKLWGG RFEASLEKWV EEFGASISFD QKMAEFDLKG SIAHVTMLGE TGIIAQEEAL
QIKQGLEELL EEYKAGKLEF DVSNEDIHMN IESLLTAKIG PVAGKLHTAR SRNDQVATDM
HLYLKAKLVE VIEKIDNLRN TLVSLADKHT YTIMPGYTHL QHAQPISFGH HLMAYYNMFT
RDSERFEFNI KHTDISPLGA AALAGTTFPI DRNMTSDLMG FAKPYSNSLD AVSDRDFILE
FLSNSSILMM HMTRICEEII NWCSNEFKFV TLSDTFSTGS SIMPQKKNPD MAELIRGKSG
RVYGNLIGLL TVMKSLPLAY NKDLQEDKEG MFDTVETITV AIDILAGMLN TMTVNDKHMA
ESTEKDFSNA TELADYLATK GLPFREAHEI VGKLVLECTK AGYYLQDVPL ERYQEVSDLI
EEDIYETLKS HTAVERRHSL GGTGFDQVKW QIKEAQQSLN K