ID K3USY7_FUSPC Unreviewed; 430 AA.
AC K3USY7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=FPSE_04254 {ECO:0000313|EMBL:EKJ75611.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ75611.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ75611.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ75611.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
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}.
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:EKJ75611.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFNW01000084; EKJ75611.1; -; Genomic_DNA.
DR RefSeq; XP_009255647.1; XM_009257372.1.
DR AlphaFoldDB; K3USY7; -.
DR EnsemblFungi; EKJ75611; EKJ75611; FPSE_04254.
DR GeneID; 20362872; -.
DR KEGG; fpu:FPSE_04254; -.
DR eggNOG; KOG1706; Eukaryota.
DR HOGENOM; CLU_032784_4_2_1; -.
DR OrthoDB; 350199at2759; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000007978; Chromosome 3.
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 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.
PE 4: Predicted;
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:UP000007978}.
FT DOMAIN 5..184
FT /note="Arginosuccinate synthase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00764"
FT DOMAIN 193..416
FT /note="Arginosuccinate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20979"
SQ SEQUENCE 430 AA; 48479 MW; 4323E7670F033EDF CRC64;
MSKGRVCLAY SGGLDTSTIL KWLILEGYEV VCFLADVGQV EDFGAVEKKA LALSAEHMII
ENLQKEFVEQ IVFRAIQCNA IYEDRYLLGT ALARPVIARA QVRVAEKYNC NLLSHGCTER
VWHGNLKKRI MRLTYSFSQV RFELAFKACN PSIKVITPWR LPEFCEKFQG RQDLLKFAAE
NNIPVSSTPK APWSQDENLV HCSYEAGILE DPDHTPPKDL WTQTVDPLEA PDKPFDFTVH
FEKGLPVKVA TPDQEATDSV ELFKLLNKIG HDHGVGRIDI VENRWIGLKS RGCYDTPGLT
IARLAHVDLE GLVLDSKVRK LRDQFVTVEW SQCLYNGMYF SPEREWLDEA IVSAQKGVNG
QVRLRVYKGN VYVLGRSSET SSLYSQEDAS MDSLDTFSPM DSTGFIAIQS IRLEKYGAQK
AKDGQPLSQS
//
