ID A0A426PY44_9CORY Unreviewed; 1120 AA. AC A0A426PY44; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 07-APR-2021, entry version 7. DE RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210}; DE EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210}; DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210}; GN Name=carB {ECO:0000256|HAMAP-Rule:MF_01210, GN ECO:0000313|EMBL:RRO86273.1}; GN ORFNames=CXF48_07605 {ECO:0000313|EMBL:RRO86273.1}; OS Corynebacterium bovis. OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae; OC Corynebacterium. OX NCBI_TaxID=36808 {ECO:0000313|EMBL:RRO86273.1, ECO:0000313|Proteomes:UP000276526}; RN [1] {ECO:0000313|EMBL:RRO86273.1, ECO:0000313|Proteomes:UP000276526} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=F6900 {ECO:0000313|EMBL:RRO86273.1, RC ECO:0000313|Proteomes:UP000276526}; RA Gulvik C.A.; RT "Twenty Corynebacterium bovis Genomes."; RL Submitted (JAN-2018) 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; CC Evidence={ECO:0000256|ARBA:ARBA00001777, ECO:0000256|HAMAP- CC Rule:MF_01210}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl CC phosphate from bicarbonate: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01210}. 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_01210}. 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_01210}. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|ARBA:ARBA00009799, CC ECO:0000256|HAMAP-Rule:MF_01210}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01210}. 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:RRO86273.1}. 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; PQNK01000011; RRO86273.1; -; Genomic_DNA. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000276526; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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 CDD; cd01424; MGS_CPS_II; 1. DR Gene3D; 1.10.1030.10; -; 1. DR Gene3D; 3.40.50.1380; -; 1. DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR006275; CarbamoylP_synth_lsu. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR036914; MGS-like_dom_sf. DR InterPro; IPR033937; MGS_CPS_CarB. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR Pfam; PF02786; CPSase_L_D2; 2. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF02142; MGS; 1. DR PRINTS; PR00098; CPSASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF48108; SSF48108; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR SUPFAM; SSF52440; SSF52440; 2. DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1. DR PROSITE; PS50975; ATP_GRASP; 2. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 1. DR PROSITE; PS51855; MGS; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_01210}; KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP- KW Rule:MF_01210}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01210}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01210}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01210}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_01210}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01210}. FT DOMAIN 138..333 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 695..886 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 968..1120 FT /note="MGS-like" FT /evidence="ECO:0000259|PROSITE:PS51855" FT REGION 1..407 FT /note="Carboxyphosphate synthetic domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 968..1120 FT /note="Allosteric domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" SQ SEQUENCE 1120 AA; 120112 MW; 20438D62BA785D84 CRC64; MPKRPDINHV LVIGSGPIVI GQACEFDYSG TQACRVLKEE GLRVTLINSN PATIMTDPEF ADHTYIEPIQ PEYIEKIFEA ERAAGHPVDA VLATLGGQTA LNAAIQLDRR GALERHGVEL IGADIEAIER GEDRQKFKDI VARVGGASAR SRVCHTMDEV HETVAELGLP VVVRPSFTMG GLGSGLAYTD EDLDRIAGGG LAASPEANVL IEESILGWKE YELELMRDGK DNVVVVCSIE NVDALGVHTG DSVTVAPAMT LTDREFQAMR DQGIAILREV GVDTGGCNIQ FAVNPDDGRL ITIEMNPRVS RSSALASKAT GFPIAKIAAK LAIGYTLDEI RNDITEVTPA AFEPTLDYVI VKAPRFAFEK FPGADDTMTT TMKSVGEAMA VGRNYATALN KVMRSLETKE AGFWTRDDAV IAGDRATDVA AVLEDLRRPT EGRMYDIELA LRLGASVEEV HEASGVDPWF LHEVRALVEF RGTLAAAPVL DEPLLREAKF LGLSDRQIAA LRPELAGEDG VRRLRWSLGV RPVFKTVDTC AAEFEAKTPY HYSSYELDPQ AESEVAPQTE REKVIILGSG PNRIGQGIEF DYSCVHAALE LSRVGYETVM VNCNPETVST DYDTADRLYF EPLTFEDVME VYHAESESGT VAGVIVQLGG QTPLGLADRL AAAGVPVVGT SPEAINLAED RGEFGAVLER AGLPAPAYGT ATSFDEARAV ADRIGYPVLV RPSYVLGGRG MEIVYDEASL SDYIDRATEI TTDHPVLVDR FLDNAIEIDV DALCDGEEVY LAGVMEHIEE AGIHSGDSSC ALPPMTLGEG DIDTVRRSTA ALAHGIGVRG LMNVQFALKD DILYVIEANP RASRTVPFVS KATGVQLAKA AARIMLGATV RELVDEGMLP GDRDGGSLPM GHPIAVKEAV MPFNRFRSPD GKVLDSLLSP EMKSTGEVMG LDADFGTAFA KSQEGAFGPV PTSGTIFVSV ANRDKRTLIL PIQRLHSMGF EILATHGTAG MLRRNGVDCT VVAKQSDAEA TGGRSIVDDI REGRVDLVLN TPAGSAGARH DGYDIRAAAV NVGVPCITTV QGAVAVVQAI EALMDTETVV RAIQDIDHDG GDRDDAGETR //