CARA_RHOBA
ID CARA_RHOBA Reviewed; 389 AA.
AC Q7UGJ6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000255|HAMAP-Rule:MF_01209};
DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01209};
DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000255|HAMAP-Rule:MF_01209};
GN Name=carA {ECO:0000255|HAMAP-Rule:MF_01209}; OrderedLocusNames=RB5179;
OS Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1).
OC Bacteria; Planctomycetes; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=243090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10527 / NCIMB 13988 / SH1;
RX PubMed=12835416; DOI=10.1073/pnas.1431443100;
RA Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W.,
RA Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R.,
RA Reinhardt R.;
RT "Complete genome sequence of the marine planctomycete Pirellula sp. strain
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003).
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:0000255|HAMAP-
CC Rule:MF_01209};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01209}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|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.
CC {ECO:0000255|HAMAP-Rule:MF_01209}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000255|HAMAP-
CC Rule:MF_01209}.
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DR EMBL; BX294141; CAD78333.1; -; Genomic_DNA.
DR RefSeq; NP_866552.1; NC_005027.1.
DR AlphaFoldDB; Q7UGJ6; -.
DR SMR; Q7UGJ6; -.
DR STRING; 243090.RB5179; -.
DR EnsemblBacteria; CAD78333; CAD78333; RB5179.
DR KEGG; rba:RB5179; -.
DR PATRIC; fig|243090.15.peg.2480; -.
DR eggNOG; COG0505; Bacteria.
DR HOGENOM; CLU_035901_2_1_0; -.
DR InParanoid; Q7UGJ6; -.
DR OMA; CFNTGMT; -.
DR OrthoDB; 662268at2; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001025; Chromosome.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 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 Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..389
FT /note="Carbamoyl-phosphate synthase small chain"
FT /id="PRO_0000227026"
FT DOMAIN 201..387
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT REGION 1..197
FT /note="CPSase"
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT ACT_SITE 360
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT ACT_SITE 362
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
SQ SEQUENCE 389 AA; 42178 MW; 858F0053E3D9677D CRC64;
MMSSPAKAAK LALEDGTVYT GTSLGAEGET TGEVVFNTSM TGYQEILTDP SYRGQLVTMT
YPEMGNYGIN SIDLENRGTS LAGFIIRNES RMHSNYRSEG SLSDYLNSQG VVGIAGIDTR
ALVRRIRSEG AMRGVLSTTD LDDASLVAKA KASPGLVGRD LVQEVMPTQL EKWTNELDDW
TIREIREAAK DASIGDDSRP HVVCMDFGMK WNIPRHLRSR GNRVTIVPGN ASADDILKMD
PDGVFLSNGP GDPEPLTYAH KAIGELLGQV PVFGICLGHQ LLSVACGAKT FKLKFGHRGA
NQPVLDLETG KVEITSQNHG FAVDDQGLPD CLEVTHRNLN DDTIAGVRHK DTGAFAVQYH
PEAAAGPHDS HYLFSRFQEQ LNEKCGVTA
