CARA_ALKHC
ID CARA_ALKHC Reviewed; 362 AA.
AC Q9K9V8;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Carbamoyl-phosphate synthase pyrimidine-specific small chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
GN Name=pyrAA; OrderedLocusNames=BH2537;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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;
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
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:0000250}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000004; BAB06256.1; -; Genomic_DNA.
DR PIR; A83967; A83967.
DR RefSeq; WP_010898688.1; NC_002570.2.
DR AlphaFoldDB; Q9K9V8; -.
DR SMR; Q9K9V8; -.
DR STRING; 272558.10175157; -.
DR MEROPS; C26.A33; -.
DR EnsemblBacteria; BAB06256; BAB06256; BAB06256.
DR KEGG; bha:BH2537; -.
DR eggNOG; COG0505; Bacteria.
DR HOGENOM; CLU_035901_2_1_9; -.
DR OMA; CFNTGMT; -.
DR OrthoDB; 662268at2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001258; 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 ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..362
FT /note="Carbamoyl-phosphate synthase pyrimidine-specific
FT small chain"
FT /id="PRO_0000112251"
FT DOMAIN 171..358
FT /note="Glutamine amidotransferase type-1"
FT REGION 1..167
FT /note="CPSase"
FT ACT_SITE 246
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 331
FT /evidence="ECO:0000250"
FT ACT_SITE 333
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 39872 MW; C7E537CA6403071C CRC64;
MKRQLILEDG SVFVGKGFGS DREMSGEVVF NTGMTGYQEM LSDPSYCGQI VTLTYPLIGN
YGINRDDFES MNPAIHGLIV KEACDIPSNW RSEESLDSLL KAKQIPGLSG IDTRKLTRLI
RMHGTLKGQL CPLDVDVEQI VQELKATPTP TDQVSRVSTR DPYHVPGPGK RVVLVDYGMK
HNILQELIRR NCEVFVVPYH TSAEEVLRLG PDGVLLSNGP GNPEDVSEGV EMIRNLLGKV
PLFGICLGHQ LFALACGAKT EKLRFGHRGS NHPVRERSTG LIEITAQNHG YTVTEGSLVN
TDLIVTHEAV NDGTIEGLAH KVHPAFSVQY HPEASPGPED SNVLFDRFIK LMESNKHRAL
TV
