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Database: UniProt
Entry: A0A142ME56_AMIAI
LinkDB: A0A142ME56_AMIAI
Original site: A0A142ME56_AMIAI 
ID   A0A142ME56_AMIAI        Unreviewed;       504 AA.
AC   A0A142ME56;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-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=FHS67_004741 {ECO:0000313|EMBL:MBB3708401.1};
OS   Aminobacter aminovorans (Chelatobacter heintzii).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Aminobacter.
OX   NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3708401.1, ECO:0000313|Proteomes:UP000577697};
RN   [1] {ECO:0000313|EMBL:MBB3708401.1, ECO:0000313|Proteomes:UP000577697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3708401.1,
RC   ECO:0000313|Proteomes:UP000577697};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2020) 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:MBB3708401.1}.
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DR   EMBL; JACICB010000019; MBB3708401.1; -; Genomic_DNA.
DR   RefSeq; WP_067967712.1; NZ_JACICB010000019.1.
DR   AlphaFoldDB; A0A142ME56; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000577697; 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; 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.
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          53..307
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          372..448
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   504 AA;  55231 MW;  92C4FDE174B8917F CRC64;
     MSELNPRLSD KSVFPDPVYK ETVLRPLFDG AKTHHVDGFR AIDRAHLVML TETGILDAKQ
     ASAIAGALEA IDREVDPEKL VYTGEVEDFF FLIEKELKAR LGADVAGRLH TSRSRNDIDH
     TLFKLGLKQR IDALMVKARH LLAAMIDAAE REKATLIVAY THGQPAQPST FGHYLSAAIE
     VLLRDIERFE EARKIVDLSP MGAAAITTSG FPIDRQRVAD LLGFAAPLRN SYSCIAASDY
     ITSTYSAIEL MFLHLGRLIQ DFQFWTSFEV GQVYVPNAFV QISSIMPQKR NPVPIEHMRL
     LASQTMGRAR TVLGVIHNTP FTDMNDSEGE TQSMGYEAFT AASRVLDLLA AFVGAIRIDP
     ERVAENIRRS CITITELADS LVRIEGLTFR EAHEIAATVA KAVVAAGGGL AKDGYAPFLE
     AFRHSTGREP SFGRDKFEEI VSPEHFVAVR DRFGGPAPAA MAEAIGVYRK KAAALEAVAQ
     EHAGHEAKAA KELGEKFKAL AGAL
//
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