ID A5E6D4_LODEL Unreviewed; 464 AA.
AC A5E6D4;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Arginosuccinase {ECO:0000256|ARBA:ARBA00032749};
GN ORFNames=LELG_05173 {ECO:0000313|EMBL:EDK46992.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK46992.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK46992.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00010755}.
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DR EMBL; CH981531; EDK46992.1; -; Genomic_DNA.
DR RefSeq; XP_001523757.1; XM_001523707.1.
DR AlphaFoldDB; A5E6D4; -.
DR STRING; 379508.A5E6D4; -.
DR GeneID; 5230838; -.
DR KEGG; lel:LELG_05173; -.
DR VEuPathDB; FungiDB:LELG_05173; -.
DR eggNOG; KOG1316; Eukaryota.
DR HOGENOM; CLU_027272_2_1_1; -.
DR InParanoid; A5E6D4; -.
DR OMA; DFAIEFC; -.
DR OrthoDB; 2722228at2759; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:InterPro.
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 Lyase {ECO:0000313|EMBL:EDK46992.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001996}.
FT DOMAIN 13..308
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 371..439
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 464 AA; 52248 MW; F47EA369F303C2CD CRC64;
MSEQPSESKL WGGRFTGATD PLMDLYNASL PYDQIMYDAD LTGTKVYTEG LNKLELITDD
ELSKIHEGLE VIRKEWAEGK FVEKPGDEDI HTANERRLGE IIGKHIAGKV HTGRSRNDQV
ATDMRIYVRE SLKDLSLKLK TFIETILKRA ENEISVLMPG YTHLQRAQPI RWSHWLSSYA
TYFTEDYNRL QQIIARVNKS PLGAGALAGH PYGIDREFLA KGLGFDDVIG NSLTAVSDRD
FVVETLFWGT LFMNHISRFA EDLIIYSTAE FGFIKLADAY STGSSLMPQK KNPDSLELLR
GKSGRVFGGL SGFLMSIKSI PSTYNKDMQE DKEPLFDALT TVEHSILIAT GVISTLTINK
ERMEGALTMD MLATDLADYL VRKGVPFRET HHISGECVRK AEDENLSGID QLTFEQFKEI
DERFEKDVLD SFDFEVSVER RDALGGTAKS AVLKQLKTLK SQLE
//
