CARX_ALKHC
ID CARX_ALKHC Reviewed; 359 AA.
AC Q9K8V6;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Carbamoyl-phosphate synthase arginine-specific small chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
GN Name=carA; OrderedLocusNames=BH2896;
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: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1.
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}.
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DR EMBL; BA000004; BAB06615.1; -; Genomic_DNA.
DR PIR; H84011; H84011.
DR RefSeq; WP_010899043.1; NC_002570.2.
DR AlphaFoldDB; Q9K8V6; -.
DR SMR; Q9K8V6; -.
DR STRING; 272558.10175518; -.
DR MEROPS; C26.963; -.
DR EnsemblBacteria; BAB06615; BAB06615; BAB06615.
DR KEGG; bha:BH2896; -.
DR eggNOG; COG0505; Bacteria.
DR HOGENOM; CLU_035901_2_1_9; -.
DR OMA; SQNHSYV; -.
DR OrthoDB; 662268at2; -.
DR UniPathway; UPA00068; UER00171.
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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
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; Reference proteome.
FT CHAIN 1..359
FT /note="Carbamoyl-phosphate synthase arginine-specific small
FT chain"
FT /id="PRO_0000112252"
FT DOMAIN 168..355
FT /note="Glutamine amidotransferase type-1"
FT REGION 1..164
FT /note="CPSase"
FT ACT_SITE 243
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 328
FT /evidence="ECO:0000250"
FT ACT_SITE 330
FT /evidence="ECO:0000250"
SQ SEQUENCE 359 AA; 39969 MW; EB1B4EDF7A30B72C CRC64;
MKAYLVLATG ETFAGEIANA KEDVYGEVVF FTGMTGYQEV LSDPSFKGQL VVFTYPLIGN
YGINASDFES KEPQAAGLIV SEQSEEGHHY EATQSLQQFC DQHQLPLLTG IDTRAVVKRI
REQGDMPAVI TTDLSRVSFE EWVPLSERAL VDEVSTKKVE TFEGNGPHIV LIDYGFKQSI
LNSLLKRDCQ VTIVPYDVSF EVVQELNPDG LLFSNGPGDP KQIEDRLPTI YRLASTYPSL
GICLGHQLLA LAFGADTEKL RFGHRGANQP VINLKSNRVY MTSQNHSYVV KEDSLQRTDW
DATFKNINDG SIEGLTHKYL PIQTVQFHPE AHPGPSDSDE IFHSFIDDVA AKGREKTYA
