ID D0SAD5_ACIJO Unreviewed; 447 AA.
AC D0SAD5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=Argininosuccinate synthase {ECO:0000256|ARBA:ARBA00014810};
DE EC=6.3.4.5 {ECO:0000256|ARBA:ARBA00012286};
DE AltName: Full=Citrulline--aspartate ligase {ECO:0000256|ARBA:ARBA00029916};
GN Name=argG {ECO:0000313|EMBL:EEY97372.1};
GN ORFNames=HMPREF0016_00455 {ECO:0000313|EMBL:EEY97372.1};
OS Acinetobacter johnsonii SH046.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=575586 {ECO:0000313|EMBL:EEY97372.1, ECO:0000313|Proteomes:UP000012047};
RN [1] {ECO:0000313|Proteomes:UP000012047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH046 {ECO:0000313|Proteomes:UP000012047};
RX PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA Seifert H., Dijkshoorn L.;
RT "The success of Acinetobacter species; genetic, metabolic and virulence
RT attributes.";
RL PLoS ONE 7:E46984-E46984(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-
CC arginino)succinate + AMP + diphosphate + H(+); Xref=Rhea:RHEA:10932,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57472, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:456215; EC=6.3.4.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001891};
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00009088}.
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DR EMBL; GG704964; EEY97372.1; -; Genomic_DNA.
DR RefSeq; WP_004694013.1; NZ_GG704964.1.
DR AlphaFoldDB; D0SAD5; -.
DR GeneID; 56338697; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_1_6; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000012047; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01999; Argininosuccinate_Synthase; 1.
DR Gene3D; 1.10.287.400; -; 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; IPR024073; AS_multimer_C_tail.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EEY97372.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 16..163
FT /note="Arginosuccinate synthase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00764"
FT DOMAIN 194..410
FT /note="Arginosuccinate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20979"
SQ SEQUENCE 447 AA; 49636 MW; 75CC69CFB6B3F5AD CRC64;
MTDNATILQN VPVGKKVGIA FSGGLDTSAA LLWMKQKGAE PYAYTANLGQ PDEDDYDAIP
KKAEAYGAVK ARLVDCRLQL ALEGIAAIQC GAFHISTGGV PYFNTTPLGR AVTGTMLVTA
MKEDDVNIWG DGSTYKGNDI ERFYRYGLLT NPALKIYKPW LDQTFIDELG GRAEMSQFLI
DNGFDYKMSK EKAYSTDSNM LGATHEAKDL EYLNAGIKIV DPIMGVAFWK DDVEVKAEEV
SITFEEGFPV AINGQRIEDP VEFILEANRI GGRHGLGMSD QIENRIIEAK SRGIYEAPGM
ALLHIAYERL VTGIHNEDTI EQYRINGLRL GRLLYQGRWF DSQALMLRET AQRWVAKAIT
GTVTLELRRG NDYTIMNTES ENLTYEAERL TMEKGDSMFT PMDRIGQLTM RNLDITDTRA
KLGIYTNTGL LAVGTGSAVP QLKDKNK
//
