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Database: UniProt
Entry: A0A0D1EL14_9RHOB
LinkDB: A0A0D1EL14_9RHOB
Original site: A0A0D1EL14_9RHOB 
ID   A0A0D1EL14_9RHOB        Unreviewed;       455 AA.
AC   A0A0D1EL14;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=argH1 {ECO:0000313|EMBL:KIT16430.1};
GN   Synonyms=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN   ORFNames=jaqu_18170 {ECO:0000313|EMBL:KIT16430.1};
OS   Jannaschia aquimarina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia.
OX   NCBI_TaxID=935700 {ECO:0000313|EMBL:KIT16430.1, ECO:0000313|Proteomes:UP000032232};
RN   [1] {ECO:0000313|EMBL:KIT16430.1, ECO:0000313|Proteomes:UP000032232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GSW-M26 {ECO:0000313|EMBL:KIT16430.1,
RC   ECO:0000313|Proteomes:UP000032232};
RA   Voget S., Daniel R.;
RT   "Genome Sequence of Jannaschia aquimarina DSM28248, a member of the
RT   Roseobacter clade.";
RL   Submitted (FEB-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:KIT16430.1}.
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DR   EMBL; JYFE01000034; KIT16430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D1EL14; -.
DR   STRING; 935700.jaqu_18170; -.
DR   PATRIC; fig|935700.4.peg.1884; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000032232; 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:UP000032232}.
FT   DOMAIN          4..298
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          361..430
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   455 AA;  49525 MW;  D369D7956C3078AD CRC64;
     MWGGRFQEGP DAIMEAINAS IGFDRRMARQ DIEGSRAHAA MLAATGIVSD KDAEAIREGL
     LTVLSEIEAG TFQFSTALED IHMNVEARLT ELIGAPAGRL HTARSRNDQV ALDFRMWVRD
     QADAAVDALP RLIAALVDQA EAGADWVMPG FTHLQTAQPV TWGHHMLAYA EMFHRDLGRF
     RDARARMNEC PLGTAALAGT SFPIDREMTA KALGFDRPAA NSLDAVSDRD FALEFLSAAS
     ICAMHLSRLA EELVIWSSAQ FRFVRLSDRW STGSSIMPQK RNPDAAELLR AKLGRILGAN
     VALFTVMKGL PLTYSKDMQE DKEQVFDAAD SLMLALAAMT GMVSDMAPQR EALEAAASSG
     FSTATDLADW LVSEADLPFR EAHHVTGALV AKAEARGCDL PDLSLEEMQD AHPAITEGVF
     DVLGVHNSVA SRTSYGGTAP DNVRSQVKRW REVLP
//
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