CARA_SYNY3
ID CARA_SYNY3 Reviewed; 384 AA.
AC P74587;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 25-MAY-2022, entry version 140.
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=sll1498;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA18695.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000022; BAA18695.1; ALT_INIT; Genomic_DNA.
DR PIR; S76783; S76783.
DR AlphaFoldDB; P74587; -.
DR SMR; P74587; -.
DR IntAct; P74587; 1.
DR STRING; 1148.1653784; -.
DR PaxDb; P74587; -.
DR EnsemblBacteria; BAA18695; BAA18695; BAA18695.
DR KEGG; syn:sll1498; -.
DR eggNOG; COG0505; Bacteria.
DR InParanoid; P74587; -.
DR OMA; CFNTGMT; -.
DR PhylomeDB; P74587; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001425; 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..384
FT /note="Carbamoyl-phosphate synthase small chain"
FT /id="PRO_0000112339"
FT DOMAIN 196..381
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT REGION 1..192
FT /note="CPSase"
FT ACT_SITE 272
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 384 AA; 41817 MW; 3F3F4E33E38947D6 CRC64;
MPIAAAKPAL LVLADGTPYP GWSFGADGTT VGEVVFNTGM TGYQEVMTDP SYCGQIVTFT
YPELGNTGVN AEDEESIHPH VKGVVARNIT RRPSNWRSTQ SLPDYLVEHK IIGIYGIDTR
ALTRKLRSIG AMNGGISTEI LEPEALLHHI QAAPSMAGLN LVKEVTTHEV YEWTDSTNDH
WQFGPVAEQQ GQPPLTVVAL DFGVKRNILR RLASYGCRVI VVPASTSAAE ILQYNPDGIF
LSNGPGDPSA VEEGIVTTKE LLAAKKPMFG ICMGHQVLGL SLGAETFKLK FGHRGLNQPC
GLEQQVEITS QNHGFAVTEG SLAEEVEITH FNLNDKTVAG LRHKELPFFS VQYHPEASPG
PHDADYLFEK FVKLMRQQKA EVAG
