ID E4QBA0_CALH1 Unreviewed; 405 AA.
AC E4QBA0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Argininosuccinate synthase {ECO:0000256|ARBA:ARBA00012286, ECO:0000256|HAMAP-Rule:MF_00005};
DE EC=6.3.4.5 {ECO:0000256|ARBA:ARBA00012286, ECO:0000256|HAMAP-Rule:MF_00005};
DE AltName: Full=Citrulline--aspartate ligase {ECO:0000256|ARBA:ARBA00029916, ECO:0000256|HAMAP-Rule:MF_00005};
GN Name=argG {ECO:0000256|HAMAP-Rule:MF_00005,
GN ECO:0000313|EMBL:ADQ07193.1};
GN OrderedLocusNames=Calhy_1476 {ECO:0000313|EMBL:ADQ07193.1};
OS Caldicellulosiruptor hydrothermalis (strain DSM 18901 / VKM B-2411 / 108).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632292 {ECO:0000313|EMBL:ADQ07193.1, ECO:0000313|Proteomes:UP000006890};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=108;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor hydrothermalis 108.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ07193.1, ECO:0000313|Proteomes:UP000006890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18901 / VKM B-2411 / 108
RC {ECO:0000313|Proteomes:UP000006890};
RX PubMed=21216991; DOI=10.1128/JB.01515-10;
RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL J. Bacteriol. 193:1483-1484(2011).
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00005};
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, ECO:0000256|HAMAP-Rule:MF_00005}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005}.
CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type 1
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00005}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00005}.
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DR EMBL; CP002219; ADQ07193.1; -; Genomic_DNA.
DR RefSeq; WP_013403364.1; NC_014652.1.
DR AlphaFoldDB; E4QBA0; -.
DR STRING; 632292.Calhy_1476; -.
DR KEGG; chd:Calhy_1476; -.
DR eggNOG; COG0137; Bacteria.
DR HOGENOM; CLU_032784_4_2_9; -.
DR OrthoDB; 9801641at2; -.
DR UniPathway; UPA00068; UER00113.
DR Proteomes; UP000006890; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004055; F:argininosuccinate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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 Gene3D; 1.20.5.470; Single helix bin; 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, ECO:0000256|HAMAP-
KW Rule:MF_00005};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00005};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00005}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00005};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00005};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00005}.
FT DOMAIN 5..165
FT /note="Arginosuccinate synthase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00764"
FT DOMAIN 175..393
FT /note="Arginosuccinate synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF20979"
FT BINDING 9..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 87
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 92
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 119
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 123
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 123
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 124
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 127
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 176
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 185
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 262
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
FT BINDING 274
FT /ligand="L-citrulline"
FT /ligand_id="ChEBI:CHEBI:57743"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00005"
SQ SEQUENCE 405 AA; 45645 MW; 97E34AC52090EFAE CRC64;
MKLNKVVLAY SGGLDTSVII PWLKENFDCE VIAVVVDVGQ EDDFEAIKEK AYKTGASKVY
IEDAKEEFVN EYIFPTLKAG AIYEGKYLLG TSMARPLIAK KLVNIAKKEN ADAIAHGATG
KGNDQVRFEV TIKALMPQIK IIAPWRIWNL KSREDELNYL AQKGIDIPFK KEESYSMDGN
IWHLSHEGLD LEDPWNMPDF DKVLKITKNP LKLADSPETV EIEFEKGIPV KVNGQQMNGV
ELLKTLNKIG ANHGIGIADI VENRLVGMKS RGVYETPGGT ILYYAHRELE YLCLDRATLH
FKDMVAIRFA ELVYDGLWFS PLREALSAFV DKTQEVVNGT VKLVLYRGNI YSAGSKSPNS
LYIKDLATFE EDQMYNQKDA EGFINLFGLP LKVFGMVNRK EDEEN
//
