GenomeNet

Database: UniProt
Entry: G0EMA4_BRAIP
LinkDB: G0EMA4_BRAIP
Original site: G0EMA4_BRAIP 
ID   G0EMA4_BRAIP            Unreviewed;       361 AA.
AC   G0EMA4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000256|HAMAP-Rule:MF_01209};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01209};
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000256|HAMAP-Rule:MF_01209};
GN   Name=carA {ECO:0000256|HAMAP-Rule:MF_01209,
GN   ECO:0000313|EMBL:AEM22875.1};
GN   OrderedLocusNames=Bint_2269 {ECO:0000313|EMBL:AEM22875.1};
OS   Brachyspira intermedia (strain ATCC 51140 / PWS/A) (Serpulina intermedia).
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=1045858 {ECO:0000313|EMBL:AEM22875.1, ECO:0000313|Proteomes:UP000008522};
RN   [1] {ECO:0000313|EMBL:AEM22875.1, ECO:0000313|Proteomes:UP000008522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51140 / PWS/A {ECO:0000313|Proteomes:UP000008522};
RX   PubMed=21816042; DOI=10.1186/1471-2164-12-395;
RA   Hafstrom T., Jansson D.S., Segerman B.;
RT   "Complete genome sequence of Brachyspira intermedia reveals unique genomic
RT   features in Brachyspira species and phage-mediated horizontal gene
RT   transfer.";
RL   BMC Genomics 12:395-395(2011).
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         Evidence={ECO:0000256|ARBA:ARBA00001777, ECO:0000256|HAMAP-
CC         Rule:MF_01209};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01209}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01209}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|ARBA:ARBA00007800,
CC       ECO:0000256|HAMAP-Rule:MF_01209}.
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; CP002874; AEM22875.1; -; Genomic_DNA.
DR   RefSeq; WP_014488687.1; NC_017243.1.
DR   AlphaFoldDB; G0EMA4; -.
DR   KEGG; bip:Bint_2269; -.
DR   PATRIC; fig|1045858.4.peg.2272; -.
DR   eggNOG; COG0505; Bacteria.
DR   HOGENOM; CLU_035901_2_1_12; -.
DR   OMA; CFNTGMT; -.
DR   OrthoDB; 9804328at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000008522; 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-UniRule.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 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   NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR   PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01209};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01209};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01209}; Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}.
FT   DOMAIN          1..131
FT                   /note="Carbamoyl-phosphate synthase small subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   REGION          1..170
FT                   /note="CPSase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT   ACT_SITE        246
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        333
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   361 AA;  40251 MW;  D125013233239E3F CRC64;
     MKRYLILEDG SHYEGIGFGA DNFKVGELVF NTSMTGYQEV LSDLSYCGQI TVMTYPLIGN
     YGINRDDFES LNPAIFGLIV KEACKSPNNF RNSQTIDEFL KLKNIPAIEN IDTRAITKKI
     REIGTLKAVM SDTIENKDDI VKMLKETPYM NDHVKMVSTK NAFPIPNRGK KVVLIDFGAK
     LGIIRELSKR NCDLIVVPYD TDFKTIMSLN PDGIMLSNGP GNPKDVKESI NTIKELIGKV
     PIFGICLGHQ LISLACGADT IKLKFGHRGG NHPVKDLETG RISITSQNHS YAVKKESLSN
     TDLIMTHISL NDGSCEGVKH KKYPVFSVQY HPESNPGPED SKYLFDNFID MINNNYGEKN
     A
//
DBGET integrated database retrieval system