ID I0IR87_LEPFC Unreviewed; 468 AA.
AC I0IR87;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=LFE_2113 {ECO:0000313|EMBL:BAM07786.1};
OS Leptospirillum ferrooxidans (strain C2-3).
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=1162668 {ECO:0000313|EMBL:BAM07786.1, ECO:0000313|Proteomes:UP000007382};
RN [1] {ECO:0000313|EMBL:BAM07786.1, ECO:0000313|Proteomes:UP000007382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-3 {ECO:0000313|EMBL:BAM07786.1,
RC ECO:0000313|Proteomes:UP000007382};
RX PubMed=22815442; DOI=10.1128/JB.00696-12;
RA Fujimura R., Sato Y., Nishizawa T., Oshima K., Kim S.-W., Hattori M.,
RA Kamijo T., Ohta H.;
RT "Complete Genome Sequence of Leptospirillum ferrooxidans Strain C2-3,
RT Isolated from a Fresh Volcanic Ash Deposit on the Island of Miyake,
RT Japan.";
RL J. Bacteriol. 194:4122-4123(2012).
RN [2] {ECO:0000313|Proteomes:UP000007382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2-3 {ECO:0000313|Proteomes:UP000007382};
RA Fujimura R., Sato Y., Nishizawa T., Nanba K., Oshima K., Hattori M.,
RA Kamijo T., Ohta H.;
RT "The complete genome sequence of the pioneer microbe on fresh volcanic
RT deposit, Leptospirillum ferrooxidans strain C2-3.";
RL Submitted (MAR-2012) 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; AP012342; BAM07786.1; -; Genomic_DNA.
DR AlphaFoldDB; I0IR87; -.
DR STRING; 1162668.LFE_2113; -.
DR KEGG; lfc:LFE_2113; -.
DR PATRIC; fig|1162668.3.peg.2503; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_0; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000007382; 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; 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:BAM07786.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007382}.
FT DOMAIN 15..309
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 373..439
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 468 AA; 51988 MW; 8AC5BCF2AA898008 CRC64;
MMEKGAPLPD KPWGGRFQEA TDEEVLAYTE SISFDQTLWR QDIRGSGAHA KMLVKVGILT
GEEGDAILLG LSEIAEEFEK GTFPVRPELE DIHMNIERRL FEKIGTPAHK LHTARSRNDQ
VALDLRLYVV DEASALVGLL RDLLDVILEK AEGGVDLLMP GYTHLQPAQP ITGGYYYLCH
AERLLRDLDR VKDVRRRAGI SPLGSGALAG TTFPIDRHYV ADLLGLQGIT GNGLDAVSDR
DFAADFLHAL SLLMVHLSQW AEEWILWSTS EFSVLEIPDR YMTGSSMMPQ KKNPDILELT
RGRAGRVLGD YVSLMTLLKA LPGGYNRDLQ EDKEQLFDAV SVGKRAVSMM TSLCGQARLK
EEKLRSRLSS GGLLATDMAE DLVRMGVPFR EAHAIVGRIV AHSDKLGLSL SEMSDEDLSR
FYEGFPKGYA KCLTPEMAVS RRNHPGGPAR ERVLERISAI RSILAEFR
//
