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Database: UniProt
Entry: A0A0D2D4B3_9EURO
LinkDB: A0A0D2D4B3_9EURO
Original site: A0A0D2D4B3_9EURO 
ID   A0A0D2D4B3_9EURO        Unreviewed;       465 AA.
AC   A0A0D2D4B3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Arginosuccinase {ECO:0000256|ARBA:ARBA00032749};
GN   ORFNames=PV05_05791 {ECO:0000313|EMBL:KIW57202.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW57202.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW57202.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW57202.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000256|ARBA:ARBA00010755}.
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DR   EMBL; KN847319; KIW57202.1; -; Genomic_DNA.
DR   RefSeq; XP_013317786.1; XM_013462332.1.
DR   AlphaFoldDB; A0A0D2D4B3; -.
DR   STRING; 348802.A0A0D2D4B3; -.
DR   GeneID; 25327699; -.
DR   HOGENOM; CLU_027272_2_1_1; -.
DR   OrthoDB; 2722228at2759; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000054342; 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:KIW57202.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT   DOMAIN          14..310
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          373..440
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   465 AA;  51843 MW;  C634D8C2CA842F02 CRC64;
     MTASKPSANM LWGGRFTGGL DPLMVSYNES IYFDRAIYAQ DIRGSIAYAR ANAKIGILTQ
     DEFEAIEKGF GQVLSEWQDD KFEIKPGVDE DIHTANERRL GEIIGTQIAG KLHTGRSRND
     QVGTGMRLWL RDQLREIEQH LIALLRVTTS RAQSEISALM PGYTHLQRAQ PIRWSHWLLS
     YGTVFTSDLE RLREVTRRVN RSPLGSGALV GNPFGIDREA MAKELGFESI INNSMAAVGD
     RDFVVETLQW AATLMQHISR WAEDLILYST AEFGFVRLAD AYSTGSSLMP QKKNPDSLEL
     LRGKSGRVFG YMAGLMMSVK GLPSTYNKDL QESFEPMLDG VKTTADSIQI ATGVLSTLTI
     FPDKMKAALT PDMLATDLAD YLVRKGVPFR ETHHISGRVV ALAEQEGKPM DQLSLQQLQG
     VDSRFGDDVM DAFNYEASVE KRTVLGGTSR KSVEEQISRI QKMLE
//
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