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Database: UniProt
Entry: A0A3S2UJ10_9RHOB
LinkDB: A0A3S2UJ10_9RHOB
Original site: A0A3S2UJ10_9RHOB 
ID   A0A3S2UJ10_9RHOB        Unreviewed;       466 AA.
AC   A0A3S2UJ10;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
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   ECO:0000313|EMBL:RVT87238.1};
GN   ORFNames=DXV76_03930 {ECO:0000313|EMBL:RVT87238.1};
OS   Rhodobacteraceae bacterium CCMM004.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=2499834 {ECO:0000313|EMBL:RVT87238.1, ECO:0000313|Proteomes:UP000287438};
RN   [1] {ECO:0000313|EMBL:RVT87238.1, ECO:0000313|Proteomes:UP000287438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMM004 {ECO:0000313|EMBL:RVT87238.1,
RC   ECO:0000313|Proteomes:UP000287438};
RA   Zhang Z.;
RT   "Salalgibacter marinus gen. nov., sp. nov., isolated from a Synechococcus
RT   culture.";
RL   Submitted (JAN-2019) 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:RVT87238.1}.
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DR   EMBL; RZWH01000001; RVT87238.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S2UJ10; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000287438; 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|HAMAP-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:UP000287438}.
FT   DOMAIN          12..306
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          369..437
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   466 AA;  49928 MW;  5DBC7727511AE6C4 CRC64;
     MTDQAANAMW GGRFAAGPDA IMEAINASIG FDRRLAAQDI AGSRAHAAML AATGIVEASE
     AEAMRKGLLT VLSEIEDGTF QFSTALEDIH MNVEARLREL IGPAAGRLHT ARSRNDQVAT
     DFRLWVRDQC DAAAQGIAEV QRALLGQAEA GADWVMPGFT HLQTAQPVTW GHHMLAYVEM
     LGRDAGRFAD ARVRMNECPL GAAALAGTSF PIDRQMTAEA LGFDRPCANS LDAVSDRDFA
     LEFLAAASIC AMHLSRLAEE LVIWSSAQFR FVTMSDRWST GSSIMPQKKN PDAAELIRAK
     IGRILGANIA LLTVMKGLPL TYSKDMQEDK EQVFDAADTL MLALAAMAGM VADMTANRDA
     LAAAAGAGFS TATDLADWLV RTLGLPFRDA HHVTGALVAR AEARGVDLAD LSLDEMQAVH
     AEIDEGVFDV LGVENSVGSR TSYGGTAPVR VREQIARWRA ALPVET
//
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