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
//