ID G6E6R4_9SPHN Unreviewed; 388 AA. AC G6E6R4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 27-SEP-2017, entry version 34. 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 ORFNames=NSU_0035 {ECO:0000313|EMBL:EHJ62960.1}; OS Novosphingobium pentaromativorans US6-1. OC Bacteria; Proteobacteria; 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: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01209}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01209}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {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 CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC {ECO:0000256|HAMAP-Rule:MF_01209}. CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|HAMAP- CC Rule:MF_01209}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 EnsemblBacteria; EHJ62960; EHJ62960; NSU_0035. DR KEGG; npn:JI59_00650; -. DR PATRIC; fig|1088721.3.peg.35; -. DR KO; K01956; -. DR OrthoDB; POG091H01NP; -. 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-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; 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 {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 Complete proteome {ECO:0000313|Proteomes:UP000004030}; KW Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01209}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01209}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}; KW Reference proteome {ECO:0000313|Proteomes:UP000004030}. FT DOMAIN 205 388 Glutamine amidotransferase type-1. FT {ECO:0000259|PROSITE:PS51273}. FT REGION 1 204 CPSase. {ECO:0000256|HAMAP-Rule: FT MF_01209}. FT ACT_SITE 282 282 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01209}. FT ACT_SITE 366 366 {ECO:0000256|HAMAP-Rule:MF_01209}. FT ACT_SITE 368 368 {ECO:0000256|HAMAP-Rule:MF_01209}. 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 //