ID A0A166ILK8_9MICO Unreviewed; 480 AA.
AC A0A166ILK8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:KZX22582.1};
GN ORFNames=ACH61_00212 {ECO:0000313|EMBL:KZX22582.1}, EV639_11185
GN {ECO:0000313|EMBL:TCO34816.1};
OS Rathayibacter tanaceti.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=1671680 {ECO:0000313|EMBL:KZX22582.1, ECO:0000313|Proteomes:UP000076717};
RN [1] {ECO:0000313|EMBL:TCO34816.1, ECO:0000313|Proteomes:UP000295366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:TCO34816.1,
RC ECO:0000313|Proteomes:UP000295366};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
RN [2] {ECO:0000313|EMBL:KZX22582.1, ECO:0000313|Proteomes:UP000076717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:KZX22582.1,
RC ECO:0000313|Proteomes:UP000076717};
RA Vasilenko O.V., Starodumova I.P., Tarlachkov S.V., Dorofeeva L.V.,
RA Evtushenko L.I.;
RT "Draft Genome Sequence of Rathayibacter sp. Strain VKM Ac-2596 Isolated
RT from Leaf Gall Induced by Plant-Parasitic Nematodes.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TCO34816.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VKM Ac-2596 {ECO:0000313|EMBL:TCO34816.1};
RA Whitman W., Huntemann M., Clum A., Pillay M., Palaniappan K., Varghese N.,
RA Mikhailova N., Stamatis D., Reddy T., Daum C., Shapiro N., Ivanova N.,
RA Kyrpides N., Woyke T.;
RL Submitted (MAR-2019) 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:KZX22582.1}.
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DR EMBL; LIIN01000004; KZX22582.1; -; Genomic_DNA.
DR EMBL; SLWP01000011; TCO34816.1; -; Genomic_DNA.
DR RefSeq; WP_068207469.1; NZ_SLWP01000011.1.
DR AlphaFoldDB; A0A166ILK8; -.
DR PATRIC; fig|1671680.3.peg.225; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000076717; Unassembled WGS sequence.
DR Proteomes; UP000295366; 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|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:KZX22582.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076717}.
FT DOMAIN 25..313
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 376..444
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 480 AA; 51038 MW; 454C30F91FDB152C CRC64;
MTERPSARAG EAGALWGGRF AGGPSPELAA LSKSTHFDWQ LAPYDLAGSR AHARALAAAG
YLDEAELMGM LDALDRLGTA VADGSFTAEE ADEDVHGALE RGLMLEAGPA LGGKLRAGRS
RNDQIATFVR MYLRDHAVIV SELVVQLIDA LAAQATAHPT AIMPGRTHLQ HAQPVLLAHH
LLAHGWALLR DLERLRDWTA RADVSPYGSG ALAGSTLGLD AEAVARDLGF AESVPNSIDG
TASRDLVAEF AFVAAMVGVD VSRIAEEVIL WNTREFAFVT LDDGYSTGSS IMPQKKNPDI
AELARGKAGR LLGNLTGLLA TLKALPLAYN RDLQEDKEPV FDSVTTLEVL LPAFSGMIAT
LTFHTDRMAE LAPQGFSLAT DVAEWLVKKH VPFRDAHEIT GELVKLAESR GLGLDGLDDD
TLASVSPSLT PDVRSVLSIE GSVASRDGVG GTAPDRVAEQ LGRLTERVRV VRAALRGERA
//