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Database: UniProt
Entry: A0A0W8I142_9MICO
LinkDB: A0A0W8I142_9MICO
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ID   A0A0W8I142_9MICO        Unreviewed;       473 AA.
AC   A0A0W8I142;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ORFNames=AVL62_08790 {ECO:0000313|EMBL:KUG51440.1};
OS   Serinicoccus chungangensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Ornithinimicrobiaceae; Serinicoccus.
OX   NCBI_TaxID=767452 {ECO:0000313|EMBL:KUG51440.1, ECO:0000313|Proteomes:UP000054837};
RN   [1] {ECO:0000313|EMBL:KUG51440.1, ECO:0000313|Proteomes:UP000054837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD08_5 {ECO:0000313|EMBL:KUG51440.1,
RC   ECO:0000313|Proteomes:UP000054837};
RA   Chander A.M., Kaur G., Nair G.R., Dhawan D.K., Kochhar R.K., Mayilraj S.,
RA   Bhadada S.K.;
RT   "Serinicoccus chungangenesis strain CD08_5 genome sequencing and
RT   assembly.";
RL   Submitted (DEC-2015) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000985, 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUG51440.1}.
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DR   EMBL; LQBL01000032; KUG51440.1; -; Genomic_DNA.
DR   RefSeq; WP_058892336.1; NZ_LQBL01000032.1.
DR   AlphaFoldDB; A0A0W8I142; -.
DR   STRING; 767452.AVL62_08790; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000054837; Unassembled WGS sequence.
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; 1.10.40.30; 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|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:KUG51440.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054837}.
FT   DOMAIN          8..303
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          366..433
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   473 AA;  50896 MW;  DCBFFC91AA94287E CRC64;
     MTVSLWGGRF TGGPSDALAA LSKSTHFDWR LAPYDLAGSR AHARVLHRAG LLSDEDLEAM
     LAALGQLLAD LGSGEFVALD TDEDVHTALE RGLIERAGPE VGGRLRAGRS RNDQVAAQFR
     MYLRDQARLL GARVLEVVQA LVDQAATHPE VAMPGRTHLQ HAQPVLLAHH LQAHAWALVR
     DVERLVDWDQ RAAVSPYGSG ALAGSSLGLD PQSVAHDLGM PRAVDNSIDG TASRDFAAEF
     SFVMAMTAVD LSRIAEEVIL WATAEFGFVT LDDAFSTGSS IMPQKKNPDV AELARGKAGR
     LIGDLAGLLA TLKGLPLAYN RDLQEDKEPV FDAVDTLEVL LPAVSGMVAT LTFHPGRLEE
     LAPQGFSLAT DVAEWLVREG VPFRVAHEVA GACVRHCEER GMGLEDLDDA ALASISPHLH
     PGVRSVLTVP GSLASRNAHG GTAPVRVTEQ RAHLLKQLAR LRHWVREMPA IRD
//
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