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Database: UniProt
Entry: A0A0A0D0J7_9PROT
LinkDB: A0A0A0D0J7_9PROT
Original site: A0A0A0D0J7_9PROT 
ID   A0A0A0D0J7_9PROT        Unreviewed;       474 AA.
AC   A0A0A0D0J7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
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=P409_26580 {ECO:0000313|EMBL:KGM31544.1};
OS   Inquilinus limosus MP06.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Inquilinus.
OX   NCBI_TaxID=1398085 {ECO:0000313|EMBL:KGM31544.1, ECO:0000313|Proteomes:UP000029995};
RN   [1] {ECO:0000313|EMBL:KGM31544.1, ECO:0000313|Proteomes:UP000029995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP06 {ECO:0000313|EMBL:KGM31544.1,
RC   ECO:0000313|Proteomes:UP000029995};
RA   Pino M., Di Conza J., Gutkind G.;
RT   "Genome sequence determination for a cystic fibrosis isolate, Inquilinus
RT   limosus.";
RL   Submitted (JAN-2014) 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:KGM31544.1}.
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DR   EMBL; JANX01000487; KGM31544.1; -; Genomic_DNA.
DR   RefSeq; WP_034845522.1; NZ_JANX01000487.1.
DR   AlphaFoldDB; A0A0A0D0J7; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000029995; 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}.
FT   DOMAIN          23..317
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          380..449
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  51350 MW;  14F930EA05C7F124 CRC64;
     MSDPTQPATP VVPDKGTNPM WGGRFAGGPA AIMERINASI GFDRKLWAQD IAGSRAHVAM
     LAAQGIVSAE DAAAIDRGLE QIAGEIAEGR FEFKTALEDI HFNVESRLTE IIGPAAGRLH
     TARSRNDQVA TDFRLWVRDA FDRLEQGLQA LQAALIAQAE QHVDTILPGF THLQVAQPVT
     FGHHLLAYVE MLGRDRSRVA DARARANECP LGAAALAGTP YPIDRHATAK ALGFDRPTAN
     SLDSVSDRDF ALDYLATAGI CAMHLSRLAE EIVFWSTPQF RFVRLSDGFS TGSSIMPQKR
     NPDAAELVRG KTGRVFGGLG ALLTVMKGLP LTYQKDMQED KEPVFDADDT LMLCLAAMTG
     MVESWTVNAE AMRRATEAGF PTATDLADWL VRQLGVPFRE AHHITGHLVK LAEDKGCRLS
     ELPLAEMQAV HPGITDAVYA VLTAEASVAS RKSYGGTAPD RVREAVQAAK ERFL
//
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