ID A0A164V208_BACCE Unreviewed; 365 AA. AC A0A164V208; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 07-SEP-2016, entry version 2. 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=B4155_3100 {ECO:0000313|EMBL:KZD81153.1}; OS Bacillus cereus. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1396 {ECO:0000313|EMBL:KZD81153.1, ECO:0000313|Proteomes:UP000076594}; RN [1] {ECO:0000313|EMBL:KZD81153.1, ECO:0000313|Proteomes:UP000076594} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B4155 {ECO:0000313|EMBL:KZD81153.1, RC ECO:0000313|Proteomes:UP000076594}; RA Boekhorst J.; RT "Bacillus cereus food isolates."; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. 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 -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000256|HAMAP-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:KZD81153.1}. 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; LJKJ01000056; KZD81153.1; -; Genomic_DNA. DR RefSeq; WP_000828686.1; NZ_LJKJ01000056.1. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000076594; Unassembled WGS sequence. 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; 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:UP000076594}; 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}. FT REGION 1 169 CPSase. {ECO:0000256|HAMAP-Rule: FT MF_01209}. FT ACT_SITE 245 245 Nucleophile. {ECO:0000256|HAMAP-Rule: FT MF_01209}. FT ACT_SITE 330 330 {ECO:0000256|HAMAP-Rule:MF_01209}. FT ACT_SITE 332 332 {ECO:0000256|HAMAP-Rule:MF_01209}. SQ SEQUENCE 365 AA; 40362 MW; 0C08E19086E4665A CRC64; MKRQLILEDG TVLIGTGFGG EIEKSGEVVF TTGMTGYQET LSDPSYCGQI VTFTYPLIGN YGINRDDFES IHPSVNGLIV NEICNHPSNF RNEISLNDYL KERNIPGLAG IDTRKLTRKI RQYGTLRGRL CNMDADVEYI VSQLKATVFT DHVKRVSTKD PYPSPGRGHR VVLVDFGMKH GILRELNKRD CDVIVVPYNT TAEEILRLSP DGIMLSNGPG DPKDVPEAIE MLKDIIGKVP LFGICLGHQL FALASGANTS KLKFGHRGLN HPVKNLATGK VAITSQNHGY AVEEESVENT DLEITHVALN DGTVEGLRHK KFPAFTVQYH PEASAGPEDA NDLFEDFLTM IENFKKEGEE LCQNA //