ID   ARLY_STRP2              Reviewed;         463 AA.
AC   Q04MW6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=SPD_0111;
OS   Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=373153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D39 / NCTC 7466;
RX   PubMed=17041037; DOI=10.1128/jb.01148-06;
RA   Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA   Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT   "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT   pneumoniae and comparison with that of unencapsulated laboratory strain
RT   R6.";
RL   J. Bacteriol. 189:38-51(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; CP000410; ABJ55243.1; -; Genomic_DNA.
DR   RefSeq; WP_001107614.1; NC_008533.2.
DR   AlphaFoldDB; Q04MW6; -.
DR   SMR; Q04MW6; -.
DR   STRING; 373153.SPD_0111; -.
DR   EnsemblBacteria; ABJ55243; ABJ55243; SPD_0111.
DR   GeneID; 60233883; -.
DR   GeneID; 66805317; -.
DR   KEGG; spd:SPD_0111; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_9; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   BioCyc; SPNE373153:G1G6V-119-MON; -.
DR   UniPathway; UPA00068; UER00114.
DR   PHI-base; PHI:4922; -.
DR   Proteomes; UP000001452; 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..463
FT                   /note="Argininosuccinate lyase"
FT                   /id="PRO_1000000548"
SQ   SEQUENCE   463 AA;  52324 MW;  936BA74D008B5121 CRC64;
     MAKNTKLWGG RFEGTVEDWV ERFGASISFD QKLAKFDVIG SLAHVQMLGQ TGILSLEESE
     KIQVGLKELL EELEAGQLDF DIANEDIHMN MEVLLTEKIG PLAGKLHTAR SRNDQVATDM
     HLYLKEQLGY VLDKLAHLKG VLLDLAENHV ATIMPGYTHL QHAQPISFAY HLMAYYNMFQ
     RDSERFEFNQ KHTDLCPLGA AALAGTTFPI DRQLSSDLLE FKQPYTNSLD AVSDRDFILE
     FLSNASILMM HMSRFCEEMI NWCSFEYQFI TLSDTFTIGS SIMPQKKNPD MAELIRGKTG
     RVYGHLFGLL TVMKSLPLAY NKDLQEDKEG MFDTVETILN SLDVLAGMLS SLQVNKEKMQ
     ESTEKDFSNA TELADYLAGK GLPFREAHEV VGRLVLDSIK SAKNLQDWTL EELQTYHSLI
     TEDIYVYLQP KTAVQRRNSL GGTGFDQVEY QIAVAKKANE AKK