CARA_PARMW
ID CARA_PARMW Reviewed; 383 AA.
AC Q7U7F9;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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}; Synonyms=pyrA;
GN OrderedLocusNames=SYNW1026;
OS Parasynechococcus marenigrum (strain WH8102).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Parasynechococcus; Parasynechococcus marenigrum.
OX NCBI_TaxID=84588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8102;
RX PubMed=12917641; DOI=10.1038/nature01943;
RA Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT "The genome of a motile marine Synechococcus.";
RL Nature 424:1037-1042(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; BX569691; CAE07541.1; -; Genomic_DNA.
DR RefSeq; WP_011127891.1; NC_005070.1.
DR AlphaFoldDB; Q7U7F9; -.
DR SMR; Q7U7F9; -.
DR STRING; 84588.SYNW1026; -.
DR MEROPS; C26.954; -.
DR EnsemblBacteria; CAE07541; CAE07541; SYNW1026.
DR KEGG; syw:SYNW1026; -.
DR eggNOG; COG0505; Bacteria.
DR HOGENOM; CLU_035901_2_1_3; -.
DR OMA; CFNTGMT; -.
DR OrthoDB; 662268at2; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001422; 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-KW.
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.
FT CHAIN 1..383
FT /note="Carbamoyl-phosphate synthase small chain"
FT /id="PRO_0000112338"
FT DOMAIN 194..381
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT REGION 1..190
FT /note="CPSase"
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT ACT_SITE 354
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT ACT_SITE 356
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
SQ SEQUENCE 383 AA; 41105 MW; 69B7363A133D4151 CRC64;
MPHPSSRQAH LVLADGTVLT GDAFGHRGSV VGEVVFNTGM TGYQEVLTDP SYAGQLVTFT
YPELGNTGVN GDDQEADHPH ARGVIARQLA PCASNWRCSE SLDNWMERHG LVGICGVDTR
ALVRRLRDGG AINGVISSDG RSPADLLAEV RHAPSMEGLN LASQVSTTEP YEWSSPCRVG
FDQRLKQHPD LPYRVVAIDF GIKRAILDRL VAHGCAVTVL PSDADLDTVM SHQPEGVFLS
NGPGDPAAVD SGIDLARSLL ERANLPLFGI CLGHQILGLA LGGKTFKLGY GHRGLNHPCG
TSGQVEITSQ NHGFAISADS LPEPMVEVTH LNLNDRTVAA FQHRHQPVFG IQYHPEASPG
PHDADHHFGR FVALMADRRD VGG