ID L7UFT1_MYXSD Unreviewed; 454 AA.
AC L7UFT1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 OrderedLocusNames=MYSTI_05596 {ECO:0000313|EMBL:AGC46873.1};
OS Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC46873.1, ECO:0000313|Proteomes:UP000011131};
RN [1] {ECO:0000313|EMBL:AGC46873.1, ECO:0000313|Proteomes:UP000011131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC {ECO:0000313|Proteomes:UP000011131};
RX PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT fruiting myxobacterium.";
RL Genome Announc. 1:E0010013-E0010013(2013).
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; CP004025; AGC46873.1; -; Genomic_DNA.
DR RefSeq; WP_015351129.1; NC_020126.1.
DR AlphaFoldDB; L7UFT1; -.
DR STRING; 1278073.MYSTI_05596; -.
DR KEGG; msd:MYSTI_05596; -.
DR PATRIC; fig|1278073.3.peg.5677; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_7; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000011131; Chromosome.
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; 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; 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:AGC46873.1}.
FT DOMAIN 34..303
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
SQ SEQUENCE 454 AA; 49223 MW; 08A7FB78203B50D4 CRC64;
MAETLWGKGA ALDAVIHRFT VGDDPIVDLS LAPHDALGSA AHARMLGKVG LLKPEESRTL
VGALKTLHDE ARAGRFTILP EQEDGHTALE AALVERIGEP GKRIHLARSR NDQVLLATRL
FLREEVLALG AGAVKLAEAF LDFAQAHAQV PMPGYTHLRR AMPSTFGMWG MAFAEGLLEE
LEALRGVWAR LDRCPLGAAA GFGVPLPIDR EYVARLLGFS RVQRSPIDAQ NGRGRHELAV
LSWACGVANT LEKWLWDVQL YSTDEFGFLG LPDAFTTGSS IMPQKKNPDV VELARGRCRE
LRGLAHQVEA IAGGLPSSYH RDFQLLKRPT LAALTSSRSL LDVLTRLVPV LQVKADAAAR
ACDDTLYAAH HAYTLVAGGQ AFRDAYRQVG RELADGTFRP DREALTATHL GGAGNLGLPQ
AREELAAARA WLDDTHHALA TASARVWDLN NPSP
//