ID A0A165F3K9_EXIGL Unreviewed; 463 AA.
AC A0A165F3K9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 20.
DE RecName: Full=Arginosuccinase {ECO:0000256|ARBA:ARBA00032749};
GN ORFNames=EXIGLDRAFT_722835 {ECO:0000313|EMBL:KZV88311.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV88311.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV88311.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV88311.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00010755}.
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DR EMBL; KV426103; KZV88311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165F3K9; -.
DR STRING; 1314781.A0A165F3K9; -.
DR InParanoid; A0A165F3K9; -.
DR OrthoDB; 2722228at2759; -.
DR Proteomes; UP000077266; 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:KZV88311.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT DOMAIN 14..308
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 371..438
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 463 AA; 51652 MW; 99F768DCF544CD11 CRC64;
MSSDAPTKQK LWGGRFTGKT DPLMHAYNQS LRYDQRMWDA DIRGSIAYAK ALQKTGILTK
DELEKMVKGL QAVGEEWKQG IFDVKEDDED IHTANERRLS ELIGPLGGKL HTGRSRNDQV
ATDMRLWLLD ELKEVEKYLK GLIGVLVSRA ENEKDVLMPG YTHLQRAQPI RWAHLLLSYA
WSLNSDLQRL RELAPRVGVS PLGCGALAGN PFLVDRDFLA AELGFTSVAE NSLWGVSDRD
FIAEFMMWAS LAMTHLSKMS EDLIVYSTAE FGFIRLSDAY STGSSMMPQK KNPDSLELIR
GKTGRIFGNM SGFMMSLKGL PSTYNKDLQE DKEPLFDTLD TVSASLRIAE GVISTLDVDA
DKMRAALTPD MLATDLADYL VRKGVPFRET HHISGRAVAL AEAEKKPLST LTLQQLQGLC
PKFTADVKDV FDFEASIERR DAIGGPSRRM VDRQIAALRK ALA
//
