ID A0A4U0ZMT7_9DELT Unreviewed; 374 AA. AC A0A4U0ZMT7; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 25-MAY-2022, entry version 12. DE RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000256|ARBA:ARBA00019036, 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|ARBA:ARBA00030197, ECO:0000256|HAMAP-Rule:MF_01209}; GN Name=carA {ECO:0000256|HAMAP-Rule:MF_01209, GN ECO:0000313|EMBL:TKB06527.1}; GN ORFNames=FCL48_20570 {ECO:0000313|EMBL:TKB06527.1}; OS Desulforhopalus sp. IMCC35007. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales; OC Desulfocapsaceae; Desulforhopalus; unclassified Desulforhopalus. OX NCBI_TaxID=2569543 {ECO:0000313|EMBL:TKB06527.1, ECO:0000313|Proteomes:UP000308209}; RN [1] {ECO:0000313|EMBL:TKB06527.1, ECO:0000313|Proteomes:UP000308209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=IMCC35007 {ECO:0000313|EMBL:TKB06527.1, RC ECO:0000313|Proteomes:UP000308209}; RA Hwang J.C.; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP- CC Rule:MF_01209}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077, CC ECO:0000256|HAMAP-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TKB06527.1}. 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; SWCN01000025; TKB06527.1; -; Genomic_DNA. DR EnsemblBacteria; TKB06527; TKB06527; FCL48_20570. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000308209; Unassembled WGS sequence. 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. 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|HAMAP-Rule:MF_01209}; KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962, KW ECO:0000256|HAMAP-Rule:MF_01209}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01209, ECO:0000313|EMBL:TKB06527.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01209}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}; KW Reference proteome {ECO:0000313|Proteomes:UP000308209}. FT DOMAIN 1..131 FT /note="CPSase_sm_chain" FT /evidence="ECO:0000259|SMART:SM01097" FT REGION 1..189 FT /note="CPSase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT ACT_SITE 265 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT ACT_SITE 350 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT ACT_SITE 352 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" SQ SEQUENCE 374 AA; 41024 MW; 28E8972D1E719476 CRC64; MKAIIALEDG TTFEGHSFTG HGEAVGEIVF NTSLSGYQEI LTDPSYTGQI VTMTYPLIGN YGTNPEDMES AAAHPKAFLI KEYNSYPSNY RSTKPLAEFL QEYGILGVEG FDTRALVRHI RTKGAMKGIV STRDLDKEAL VKKAQEWSGL VGQDMVKKVT CTSPYGWGEN EPVAGSNFET AKKPGEKAFK VVAFDFGIKY NQLRLLQKKG CQVQVVPART DAKTVLAMEP DGIFLSNGPG DPEGVEGVVD TIRELLGKKP IFGICLGHQM LGLAYGGSAY KLKFGHRGGN QPVKDLTTGH VEITSQNHGF CIDESTLPAG EVEVTHINLN DNSLEGMRHK KYPAFSVQYH PEHAPGPHDA EYLFDRFIDM MRAV //