ID A0A2S2CXG2_9PROT Unreviewed; 476 AA.
AC A0A2S2CXG2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ECO:0000313|EMBL:AWK88967.1};
GN ORFNames=DEW08_23325 {ECO:0000313|EMBL:AWK88967.1};
OS Azospirillum thermophilum.
OG Plasmid unnamed1 {ECO:0000313|EMBL:AWK88967.1,
OG ECO:0000313|Proteomes:UP000245629}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2202148 {ECO:0000313|EMBL:AWK88967.1, ECO:0000313|Proteomes:UP000245629};
RN [1] {ECO:0000313|Proteomes:UP000245629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFH 70021 {ECO:0000313|Proteomes:UP000245629};
RC PLASMID=unnamed1 {ECO:0000313|Proteomes:UP000245629};
RA Zhao Z.;
RT "Azospirillum thermophila sp. nov., a novel isolated from hot spring.";
RL Submitted (MAY-2018) 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; CP029356; AWK88967.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2CXG2; -.
DR KEGG; azz:DEW08_23325; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000245629; Plasmid unnamed1.
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 Plasmid {ECO:0000313|EMBL:AWK88967.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245629}.
FT DOMAIN 27..319
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 382..451
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 476 AA; 52132 MW; EA77E9447C6584BA CRC64;
MSAEQTKHAP DAAKDASAAS QMWGGRFASG PAAIMEKINA SIGFDKRLAD QDIAGSKAHA
AMLARQGIIS QADADAIRDG LDRVKEEIDS GRFEFKVELE DIHMNVEARL AELIGEPAKR
LHTARSRNDQ VATDFKLWVR DAIDRADAGL KALQTALIDL AEQHADTLMP GFTHLQAAQP
VTFGHHLLAY VEMFGRDRGR LTDARARLNE CPLGSAALAG TPYPIDRFMT AEALGFNRPT
ANSLDAVSDR DFALEYLAAA SICAVHLSRF AEEIVLWCSV QFRFIRLSDA FTTGSSIMPQ
KKNPDAAELV RAKAGRVIGM LNSLLIAMKG LPLAYSKDMQ EDKEPVFEAD DTLGLCIAAM
EGMVRDMEPN REAMREATAR GFLNATDLAD WLVRELGIPF REAHHITGRA VKMAEEKRVG
LTDLSLAELQ SIEPRISEAV YPALSIESSL NSRSSYGGPA PDRVREAVKV ARERFL
//
