ID   B8HGD0_PSECP            Unreviewed;       480 AA.
AC   B8HGD0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   02-SEP-2026, entry version 105.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE   AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN   Name=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN   OrderedLocusNames=Achl_1504 {ECO:0000313|EMBL:ACL39492.1};
OS   Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS   107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS   chlorophenolicus).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Micrococcaceae; Pseudarthrobacter.
OX   NCBI_TaxID=452863 {ECO:0000313|EMBL:ACL39492.1, ECO:0000313|Proteomes:UP000002505};
RN   [1] {ECO:0000313|EMBL:ACL39492.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A6 {ECO:0000313|EMBL:ACL39492.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT   "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|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.
CC       {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
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DR   EMBL; CP001341; ACL39492.1; -; Genomic_DNA.
DR   RefSeq; WP_015936713.1; NC_011886.1.
DR   AlphaFoldDB; B8HGD0; -.
DR   STRING; 452863.Achl_1504; -.
DR   KEGG; ach:Achl_1504; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_2_11; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000002505; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01359; Argininosuccinate_lyase; 1.
DR   FunFam; 1.10.40.30:FF:000001; Argininosuccinate lyase; 1.
DR   FunFam; 1.20.200.10:FF:000015; argininosuccinate lyase isoform X2; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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   NCBIfam; TIGR00838; argH; 1.
DR   PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00006};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002505}.
FT   DOMAIN          27..316
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          379..447
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   480 AA;  51444 MW;  4F3C7D4D1C5B0265 CRC64;
     MVEPVETQKT EATNAGALWG GRFAGGPADA LAALSKSTHF DWRLARYDIA GSKAHARVLH
     KAGLLDDAEL EGMLAALTQL DEDVASGAYL PAESDEDVHG SLERGLIERA GAQLGGKLRA
     GRSRNDQVAT LGRMFLRDHA RIIARGVLAT IDALVEQAKA HQGVAMPGRT HLQHAQPVLL
     SHHLLAHAWP LLRDVQRLQD WDKRAGVSPY GSGALAGSSL GLDPEAVAAD LGFFSAAHNS
     IDGTAARDVF AEFAWVCSMI GVDLSRISEE VIFWATKEFS FVTLHDSYST GSSIMPQKKN
     PDVAELARGK AGRLIGNLTG LLATLKGLPL AYNRDLQEDK EPVFDAADTL ELLLPAVSGM
     IATLTFNRER MESLAPQGFA LATDIAEWLV RQGVPFREAH ELSGAAVKQA ESRGVELWDL
     TDDEYAAISE HLTPEVRTVL STEGSLNSRN SQGGTAPAAV ERQLAALESE LAGVREYAGQ
//