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Database: UniProt
Entry: A0A0D7AM81_9AGAR
LinkDB: A0A0D7AM81_9AGAR
Original site: A0A0D7AM81_9AGAR 
ID   A0A0D7AM81_9AGAR        Unreviewed;       426 AA.
AC   A0A0D7AM81;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=argininosuccinate synthase {ECO:0000256|ARBA:ARBA00012286};
DE            EC=6.3.4.5 {ECO:0000256|ARBA:ARBA00012286};
DE   AltName: Full=Citrulline--aspartate ligase {ECO:0000256|ARBA:ARBA00029916};
GN   ORFNames=FISHEDRAFT_63617 {ECO:0000313|EMBL:KIY52975.1};
OS   Fistulina hepatica ATCC 64428.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX   NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY52975.1, ECO:0000313|Proteomes:UP000054144};
RN   [1] {ECO:0000313|EMBL:KIY52975.1, ECO:0000313|Proteomes:UP000054144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY52975.1,
RC   ECO:0000313|Proteomes:UP000054144};
RX   PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA   Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA   Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA   LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA   Hibbett D.S.;
RT   "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT   genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL   Fungal Genet. Biol. 76:78-92(2015).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004967}.
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DR   EMBL; KN881629; KIY52975.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D7AM81; -.
DR   OrthoDB; 350199at2759; -.
DR   UniPathway; UPA00068; UER00113.
DR   Proteomes; UP000054144; Unassembled WGS sequence.
DR   GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01999; Argininosuccinate_Synthase; 1.
DR   Gene3D; 3.90.1260.10; Argininosuccinate synthetase, chain A, domain 2; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00005; Arg_succ_synth_type1; 1.
DR   InterPro; IPR048268; Arginosuc_syn_C.
DR   InterPro; IPR048267; Arginosuc_syn_N.
DR   InterPro; IPR001518; Arginosuc_synth.
DR   InterPro; IPR018223; Arginosuc_synth_CS.
DR   InterPro; IPR023434; Arginosuc_synth_type_1_subfam.
DR   InterPro; IPR024074; AS_cat/multimer_dom_body.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00032; argG; 1.
DR   PANTHER; PTHR11587; ARGININOSUCCINATE SYNTHASE; 1.
DR   PANTHER; PTHR11587:SF2; ARGININOSUCCINATE SYNTHASE; 1.
DR   Pfam; PF20979; Arginosuc_syn_C; 1.
DR   Pfam; PF00764; Arginosuc_synth; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF69864; Argininosuccinate synthetase, C-terminal domain; 1.
DR   PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1.
DR   PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054144}.
FT   DOMAIN          7..171
FT                   /note="Arginosuccinate synthase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00764"
FT   DOMAIN          180..403
FT                   /note="Arginosuccinate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20979"
SQ   SEQUENCE   426 AA;  47568 MW;  5452F0D8CA8C1BF1 CRC64;
     MASSKGRVLL AYSGGLDTSC ILAWLIEQGY EVYAFMADVG QEEDFVAAEK KALKVGAKKF
     FLEDLKREFI EELIFPAVQA NCIYENVYLL GTSLARPVIA RGMIEVADRE GCDYVSHGCT
     GKGNDQVRFE LAFYGLKPEI KVVAPWRIPE FYNRFPGRQA LLDYAAEKSI PVTQTKSKPW
     STDENLFHIS YEAGILENPN TTPPDDMWKL TTAPEEAPQT PERISIEFKG GLPVKVEVPV
     DNRTYTDPVE VFLALNALGR KHGIGRIDIV ENRFIGVKSR GCYESPGATI LRAAHIDLEG
     LTLDRNVRAL RDQFITIELG RILYNGHFFT PEREFVTSAI PASQRTVNGL VRLKLYKGNV
     VIEGRESTEG LYDEHQSSMD ELGGFEPSDA TGFIQIESIR IKKWAQANIR KGQAGVLTKD
     VYGSRA
//
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