ID ASSY_PROMT Reviewed; 400 AA.
AC Q46I72;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 01-MAY-2013, entry version 56.
DE RecName: Full=Argininosuccinate synthase;
DE EC=6.3.4.5;
DE AltName: Full=Citrulline--aspartate ligase;
GN Name=argG; OrderedLocusNames=PMN2A_1317;
OS Prochlorococcus marinus (strain NATL2A).
OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=59920;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NATL2A;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA Steglich C., Church G.M., Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP +
CC diphosphate + N(omega)-(L-arginino)succinate.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-
CC arginine from L-ornithine and carbamoyl phosphate: step 2/3.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type
CC 1 subfamily.
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DR EMBL; CP000095; AAZ58806.1; -; Genomic_DNA.
DR RefSeq; YP_292509.1; NC_007335.2.
DR HSSP; Q9X2A1; 1VL2.
DR ProteinModelPortal; Q46I72; -.
DR STRING; 59920.PMN2A_1317; -.
DR PRIDE; Q46I72; -.
DR EnsemblBacteria; AAZ58806; AAZ58806; PMN2A_1317.
DR GeneID; 3606712; -.
DR KEGG; pmn:PMN2A_1317; -.
DR PATRIC; 23026546; VBIProMar14922_2193.
DR eggNOG; COG0137; -.
DR HOGENOM; HOG000230093; -.
DR KO; K01940; -.
DR OMA; NDQFRFE; -.
DR ProtClustDB; PRK00509; -.
DR BioCyc; PMAR59920:GI1O-1344-MONOMER; -.
DR UniPathway; UPA00068; UER00113.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.90.1260.10; -; 1.
DR HAMAP; MF_00005; Arg_succ_synth_type1; 1; -.
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 PANTHER; PTHR11587; PTHR11587; 1.
DR Pfam; PF00764; Arginosuc_synth; 1.
DR TIGRFAMs; TIGR00032; argG; 1.
DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1.
DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding.
FT CHAIN 1 400 Argininosuccinate synthase.
FT /FTId=PRO_0000263951.
FT NP_BIND 10 18 ATP (By similarity).
FT BINDING 38 38 ATP; via amide nitrogen and carbonyl
FT oxygen (By similarity).
FT BINDING 89 89 Citrulline (By similarity).
FT BINDING 119 119 ATP; via amide nitrogen (By similarity).
FT BINDING 121 121 Aspartate (By similarity).
FT BINDING 125 125 Aspartate (By similarity).
FT BINDING 125 125 Citrulline (By similarity).
FT BINDING 126 126 Aspartate (By similarity).
FT BINDING 129 129 Citrulline (By similarity).
FT BINDING 177 177 Citrulline (By similarity).
FT BINDING 186 186 Citrulline (By similarity).
FT BINDING 262 262 Citrulline (By similarity).
FT BINDING 274 274 Citrulline (By similarity).
SQ SEQUENCE 400 AA; 44116 MW; 305D70454D2FBCBB CRC64;
MGKANKVVLA YSGGVDTSVC IPYLKEEYGV EHVIAFAADL GQGDELDEIK KKAISAGASQ
SLIGNLVKPF IEDFAFPAIR SNALYQGRYP LSTALARPLI AKKLVEIARE LNADGVAHGC
TGKGNDQVRF DVTIGALAPD LQLLTPAREW GMSREETIAY GEKYGIVPPV SKKNPYSIDL
NLLGRSIEAG PLEDPFQMPS EEVFGITSSI ADSPNEPEIA DILFENGYPV AINGEEMEPV
SLIKKANSLA GKHGFGRLDI IEDRVVGIKS REIYETPGLL LLIKAHQEIE SLTLPADLLD
TKSRLERQWA DLVYKGFWFS PLKEALDGFI NYSQKQVNGT VRVRLFKGNV DVIGRKSKEN
SLYISDMSTY GSEDKFNHKS AEGFIYVWGL PSRIWSWINK
//
