ID I4EZC2_9ACTN Unreviewed; 386 AA.
AC I4EZC2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Carbamoyl phosphate synthase small chain {ECO:0000256|HAMAP-Rule:MF_01209};
DE EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01209};
DE AltName: Full=Carbamoyl phosphate synthetase glutamine chain {ECO:0000256|HAMAP-Rule:MF_01209};
GN Name=carA {ECO:0000256|HAMAP-Rule:MF_01209,
GN ECO:0000313|EMBL:CCH88735.1};
GN OrderedLocusNames=MODMU_3322 {ECO:0000313|EMBL:CCH88735.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH88735.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH88735.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH88735.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
CC -!- FUNCTION: Small subunit of the glutamine-dependent carbamoyl phosphate
CC synthetase (CPSase). CPSase catalyzes the formation of carbamoyl
CC phosphate from the ammonia moiety of glutamine, carbonate, and
CC phosphate donated by ATP, constituting the first step of 2 biosynthetic
CC pathways, one leading to arginine and/or urea and the other to
CC pyrimidine nucleotides. The small subunit (glutamine amidotransferase)
CC binds and cleaves glutamine to supply the large subunit with the
CC substrate ammonia. {ECO:0000256|HAMAP-Rule:MF_01209}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01209};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01209};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077,
CC ECO:0000256|HAMAP-Rule:MF_01209}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|HAMAP-
CC Rule:MF_01209}.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of
CC heterodimers (alpha,beta)4. {ECO:0000256|HAMAP-Rule:MF_01209}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|ARBA:ARBA00007800,
CC ECO:0000256|HAMAP-Rule:MF_01209}.
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DR EMBL; FO203431; CCH88735.1; -; Genomic_DNA.
DR RefSeq; WP_014741319.1; NC_017955.1.
DR AlphaFoldDB; I4EZC2; -.
DR STRING; 477641.MODMU_3322; -.
DR KEGG; mmar:MODMU_3322; -.
DR PATRIC; fig|477641.3.peg.3141; -.
DR eggNOG; COG0505; Bacteria.
DR HOGENOM; CLU_035901_2_1_11; -.
DR OMA; CFSVQYH; -.
DR OrthoDB; 9804328at2; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000006461; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01209};
KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01209};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01209}; Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT DOMAIN 2..132
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
FT REGION 1..173
FT /note="CPSase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT ACT_SITE 252
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 342
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 344
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT BINDING 46
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 224
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 226
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 253
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 256
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 294
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 296
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT BINDING 297
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
SQ SEQUENCE 386 AA; 40320 MW; 0FDC97B360BA0661 CRC64;
MSDAILVLED GRTFRGEAYG ATGTTVGEAV FSTGMTGYQE TLTDPSYAGQ IVAMTAPHIG
NTGVNGEDDE SRRMWVAGFV VRDPARRPAN WRATGSLDDE LVAQGVVGIS GIDTRALTRH
LRDRGAMRAG ISTELGAEEL LARVTDSPSM SGADLAPGVS AAEPYVVPAV GEKRFTIAAL
DLGIKTATPR ALAELGVETH VLPATATAEQ LLEAGIDGVF VSNGPGDPAA ADYAVEAVRG
VLAARRPLFG ICFGNQILGR ALGLGTYKLR FGHRGLNQPV LDRVSGTVRV TSHNHGFAVD
APLDAAVDTP FGPVEVSHVG LNDQVVEGLR LTEAPAFSVQ FHPEAAAGPH DANPLFGRFV
DLMAAERGDA VSPPLTVQHT TGEKEA
//
