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Database: UniProt
Entry: A0A421JC18_9ASCO
LinkDB: A0A421JC18_9ASCO
Original site: A0A421JC18_9ASCO 
ID   A0A421JC18_9ASCO        Unreviewed;       462 AA.
AC   A0A421JC18;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Arginosuccinase {ECO:0000256|ARBA:ARBA00032749};
GN   ORFNames=JA9_004634 {ECO:0000313|EMBL:RLV86379.1};
OS   Meyerozyma sp. JA9.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV86379.1, ECO:0000313|Proteomes:UP000286412};
RN   [1] {ECO:0000313|EMBL:RLV86379.1, ECO:0000313|Proteomes:UP000286412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA9 {ECO:0000313|EMBL:RLV86379.1,
RC   ECO:0000313|Proteomes:UP000286412};
RA   Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT   "Physiological and comparative genomic analysis of newly identified yeasts
RT   Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT   production.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC       subfamily. {ECO:0000256|ARBA:ARBA00010755}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV86379.1}.
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DR   EMBL; NSDU01000010; RLV86379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A421JC18; -.
DR   STRING; 2028340.A0A421JC18; -.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000286412; 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:RLV86379.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286412}.
FT   DOMAIN          11..306
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          369..437
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   462 AA;  51330 MW;  8AD49EE3A4FBA6B2 CRC64;
     MSDTPAKLWG GRFTGATDPL MDLYNASLPY DKKMYAADLH GTAIYTQGLH KLGILSTDEL
     ASIQQGLKVV EKEWESGTFE EKPGDEDIHT ANERRLGEVI GKHIAGKVHT GRSRNDQVAT
     DMRIFVRETL TTLLQYLSQL IGTIVNRAGQ EIDVLMPGYT HLQRAQPIRW AHWLSSYATY
     FTEDYKRLKE LLVRVNQSPL GSGALAGHPY GIDREFLAEN LGFDGVIGNS LVAVSDRDFV
     VESLFWCSLF MNHISRFSED LIIYSTAEFG FVKLADAYST GSSLMPQKKN PDSLELLRGK
     CGRVFGSLAG FMMSIKSIPS TYNKDMQEDK EPLFDALTTV EHSILIATGV ISSLSINKEK
     MEAALTMDML ATDLADYLVM KGVPFRETHH ISGECVSQAE KLNLSGIDQL SMEQLQAIDS
     RFGDDVKDVF NFEASVERRN ATGGTAKSAV LKQLESLKKQ IN
//
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