ID N1P2Q7_YEASC Unreviewed; 420 AA.
AC N1P2Q7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=CENPK1137D_1962 {ECO:0000313|EMBL:EIW07375.1};
OS Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=889517 {ECO:0000313|EMBL:EIW07375.1};
RN [1] {ECO:0000313|EMBL:EIW07375.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CEN.PK113-7D {ECO:0000313|EMBL:EIW07375.1};
RA Nijkamp J.F., van den Broek M.A., Datema E., de Kok S., Bosman L.,
RA Luttink M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA Klaassen P., Platt D., Paddon C.J., Koetter P., van Ham R.C.,
RA Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT "De novo sequencing, assembly and analysis of the genome of the laboratory
RT strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT biotechnology.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
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; CM001536; EIW07375.1; -; Genomic_DNA.
DR AlphaFoldDB; N1P2Q7; -.
DR SMR; N1P2Q7; -.
DR HOGENOM; CLU_032784_4_2_1; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000013192; Chromosome XV.
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}.
FT DOMAIN 5..169
FT /note="Arginosuccinate synthase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00764"
FT DOMAIN 178..407
FT /note="Arginosuccinate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20979"
SQ SEQUENCE 420 AA; 46928 MW; 155E1A4775B6FA9B CRC64;
MSKGKVCLAY SGGLDTSVIL AWLLDQGYEV VAFMANVGQE EDFDAAKEKA LKIGACKFVC
VDCREDFVKD ILFPAVQVNA VYEDVYLLGT SLARPVIAKA QIDVAKQEGC FAVSHGCTGK
GNDQIRFELS FYALKPDVKC ITPWRMPEFF ERFAGRKDLL DYAAQKGIPV AQTKAKPWST
DENQAHISYE AGILEDPDTT PPKDMWKLIV DPMDAPDQPQ DLTIDFERGL PVKLTYTDNK
TSKEVSVTKP LDVFLAASNL ARANGVGRID IVEDRYINLK SRGCYEQAPL TVLRKAHVDL
EGLTLDKEVR QLRDSFVTPN YSRLIYNGSY FTPECEYIRS MIQPSQNSVN GTVRVRLYKG
NVIILGRSTK TEKLYDPTES SMDELTGFLP TDTTGFIAIQ AIRIKKYGES KKTKGEELTL
//
