ID A0A1H1TJB4_9CELL Unreviewed; 476 AA.
AC A0A1H1TJB4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN04489860_1921 {ECO:0000313|EMBL:SDS60343.1};
OS Paraoerskovia marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Paraoerskovia.
OX NCBI_TaxID=545619 {ECO:0000313|EMBL:SDS60343.1, ECO:0000313|Proteomes:UP000185663};
RN [1] {ECO:0000313|EMBL:SDS60343.1, ECO:0000313|Proteomes:UP000185663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22126 {ECO:0000313|EMBL:SDS60343.1,
RC ECO:0000313|Proteomes:UP000185663};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; LT629776; SDS60343.1; -; Genomic_DNA.
DR RefSeq; WP_029252692.1; NZ_LT629776.1.
DR AlphaFoldDB; A0A1H1TJB4; -.
DR STRING; 545619.SAMN04489860_1921; -.
DR eggNOG; COG0165; Bacteria.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000185663; Chromosome i.
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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW 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:SDS60343.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185663}.
FT DOMAIN 23..312
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 375..442
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 476 AA; 50877 MW; 57DC28F30AD1E56A CRC64;
MTETNASDSQ RVSLWGGRFA GGPADALAAL SKSTHFDWRL AGQDIAGSKA HAKVLHAAGL
LDDTELEGMH AALDRLREDV ASGAFVPAEG DEDVHTALER GLIERAGLEL GGKLRAGRSR
NDQIATLVRM YLRDESRVIV GLVLDVVDAL TEQATAAGEA AMPGRTHLQH AQPVLLAHHL
LAHAWPLLRD VDRFVDWDVR AARSPYGSGA LAGSSLGLDP AAVAAELGFD GPVENSIDGT
AARDVVAEFA FVSAMLAVDL SRLAEEVIAW ATKEFGFVRL HDSYSTGSSI MPQKKNPDVA
ELARGKAGRI IGDLTGLLAT LKGLPLAYNR DLQEDKEPVF DQVDTLEVLL PAFAGMVATL
EFDTDRMAEL APQGFSLATD IAEWLVRQGV PFRVAHEVAG SCVRVCEDRG IELWDLSDED
LADISDHLTP GVREVLSVSG SLASRDAVGG TAPARVAEQL TEAKAKAVEF RFWTEG
//
