ID G6E6R4_9SPHN Unreviewed; 388 AA. AC G6E6R4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 24-JAN-2024, entry version 58. 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|ARBA:ARBA00012738, 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 ORFNames=NSU_0035 {ECO:0000313|EMBL:EHJ62960.1}; OS Novosphingobium pentaromativorans US6-1. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ62960.1, ECO:0000313|Proteomes:UP000004030}; RN [1] {ECO:0000313|EMBL:EHJ62960.1, ECO:0000313|Proteomes:UP000004030} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=US6-1 {ECO:0000313|EMBL:EHJ62960.1, RC ECO:0000313|Proteomes:UP000004030}; RX PubMed=22275104; DOI=10.1128/JB.06476-11; RA Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.; RT "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium RT pentaromativorans US6-1."; RL J. Bacteriol. 194:907-907(2012). 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|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. CC {ECO:0000256|ARBA:ARBA00004812, ECO:0000256|HAMAP-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:EHJ62960.1}. 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; AGFM01000002; EHJ62960.1; -; Genomic_DNA. DR RefSeq; WP_007010952.1; NZ_CP009291.1. DR AlphaFoldDB; G6E6R4; -. DR STRING; 1088721.JI59_00650; -. DR KEGG; npn:JI59_00650; -. DR PATRIC; fig|1088721.3.peg.35; -. DR eggNOG; COG0505; Bacteria. DR OrthoDB; 9804328at2; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000004030; 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-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|ARBA:ARBA00022571, ECO:0000256|HAMAP- KW 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}; KW Reference proteome {ECO:0000313|Proteomes:UP000004030}. FT DOMAIN 15..145 FT /note="Carbamoyl-phosphate synthase small subunit N- FT terminal" FT /evidence="ECO:0000259|SMART:SM01097" FT REGION 1..204 FT /note="CPSase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209" FT ACT_SITE 282 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 366 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605" FT ACT_SITE 368 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209, FT ECO:0000256|PROSITE-ProRule:PRU00605" SQ SEQUENCE 388 AA; 41229 MW; 00E10755DFD1BF2C CRC64; MADAAFSLAP KPEGATGVLV LSDGHVIWGR GFGAVGNAVG EVCFNTSMTG YQEVMTDPSY AGQIVTFTFP HIGNVGVNDE DLESRVDSAV GCVVREDVTP SSNFRAEGEF GDWLAAKGKI GLAGVDTRAL TRRIRLSGAP NAVIAHDPKG EFDIPALIKK AQEWPGLEGM DLAKIVSREH QEGWEGSTWT LGQGYGRSPR DERPHVVAMD FGAKDNIFRN LVKAGARVTV VPAEATLDQV LELKPQGVFL SNGPGDPAAT GKYAVPVIQG LLERDVPIFG ICLGHQMLAL AAGASTSKMH QGHRGANHPV KRLADDVVEI TSMNHGFAVD NATLPDTIEE THVSLFDGSN CGIAIKGKKA FGVQYHPEAS PGPQDSFYLF EKFVGALA //