ID A0A1N6DBA2_9GAMM Unreviewed; 470 AA.
AC A0A1N6DBA2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05443662_0008 {ECO:0000313|EMBL:SIN68098.1};
OS Sulfurivirga caldicuralii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Sulfurivirga.
OX NCBI_TaxID=364032 {ECO:0000313|EMBL:SIN68098.1, ECO:0000313|Proteomes:UP000198461};
RN [1] {ECO:0000313|EMBL:SIN68098.1, ECO:0000313|Proteomes:UP000198461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17737 {ECO:0000313|EMBL:SIN68098.1,
RC ECO:0000313|Proteomes:UP000198461};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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 -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC Argininosuccinate lyase subfamily. {ECO:0000256|ARBA:ARBA00005552}.
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DR EMBL; FSRE01000001; SIN68098.1; -; Genomic_DNA.
DR RefSeq; WP_074200365.1; NZ_FSRE01000001.1.
DR AlphaFoldDB; A0A1N6DBA2; -.
DR STRING; 364032.SAMN05443662_0008; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000198461; 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|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:SIN68098.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198461}.
FT DOMAIN 15..309
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 372..440
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 470 AA; 52786 MW; 9CA6B7F90D506DB7 CRC64;
MSDTAASKEK LSSARLTEAT DAFVEQFTAS IDFDKRMYRQ DIQGSLAHAK MLNKVGILTD
EELADIERGL AQIQREIEAG EFQFSVAQED IHMNIEARLT QLIGITGKKL HTGRSRNDQV
ATDIRLYLRD EIDERVLPQL KRLMEGLIEQ AERYHDAIMP GFTHLQTAQP VTFGHHLLAW
FEMLYRDAER LLDARRRINT SPLGSAALAG TTYPIDRHYT AELLGFERVG ENSLDGVSDR
DFAIEFTHAA ALLMMHLSRM SEELVLWASA QFQFIDLPDR FCTGSSIMPQ KKNPDVPELV
RGKSGRVYGH LMSLLTLMKS QPLAYNKDNQ EDKEPLFDTV DTVVNSLIAF ADMVPAIRFN
REAGYEAARR GFSTATDLAD YLVKKGLPFR DAHEVVGQAV AYGIRHGKDL SEMSLQELQQ
FEPRIKADVF DVLTLEGSVA ARDHFGGTAP RQVLAAAGRA RERLQTLKTA
//
