ID W0ZDJ5_9MICO Unreviewed; 1095 AA. AC W0ZDJ5; DT 19-MAR-2014, integrated into UniProtKB/TrEMBL. DT 19-MAR-2014, sequence version 1. DT 02-JUN-2021, entry version 42. 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:CDK00934.1}; GN ORFNames=MIC448_390066 {ECO:0000313|EMBL:CDK00934.1}; OS Microbacterium sp. C448. OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Microbacterium. OX NCBI_TaxID=1177594 {ECO:0000313|EMBL:CDK00934.1, ECO:0000313|Proteomes:UP000028883}; RN [1] {ECO:0000313|EMBL:CDK00934.1, ECO:0000313|Proteomes:UP000028883} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C448 {ECO:0000313|EMBL:CDK00934.1, RC ECO:0000313|Proteomes:UP000028883}; RX PubMed=24526651; DOI=10.1128/genomeA.01113-13; RA Martin-Laurent F., Marti R., Waglechner N., Wright G.D., Topp E.; RT "Draft Genome Sequence of the Sulfonamide Antibiotic-Degrading RT Microbacterium sp. Strain C448."; RL Genome Announc. Announc.2:e01113-e01113(2014). 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 {ECO:0000256|ARBA:ARBA00004725}. 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:CDK00934.1}. 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; CBVQ010000202; CDK00934.1; -; Genomic_DNA. DR RefSeq; WP_036296273.1; NZ_HG779619.1. DR STRING; 1177594.MIC448_390066; -. DR EnsemblBacteria; CDK00934; CDK00934; MIC448_390066. DR eggNOG; COG0458; Bacteria. DR HOGENOM; CLU_000513_1_0_11; -. DR OrthoDB; 48855at2; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; -. DR Proteomes; UP000028883; 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; 2. DR PROSITE; PS00867; CPSASE_2; 2. 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}; Reference proteome {ECO:0000313|Proteomes:UP000028883}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01210}. FT DOMAIN 133..328 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 676..870 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 951..1094 FT /note="MGS-like" FT /evidence="ECO:0000259|PROSITE:PS51855" FT REGION 1..402 FT /note="Carboxyphosphate synthetic domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 951..1095 FT /note="Allosteric domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" SQ SEQUENCE 1095 AA; 117538 MW; 7DD760EFF6E365A9 CRC64; MPKRDDIKSV LVIGSGPIVI GQACEFDYSG TQACRVLREE GVRVILVNSN PATIMTDPDF ADATYIEPIT WQVIETIIAK ERPDAILPTL GGQTALNAAI ELDKHGVLEK YDVELIGANL EAINKGEDRQ IFKQLVLDSG ADVADSRICH TMDEVLAGAA ELGYPLVVRP SFTMGGLGSG FAYDERDLRR IAGAGLRDSP TTEVLLEESI LGWKEYELEL MRDTADNTVV VCSIENVDPV GVHTGDSITV APALTLTDRE YQKMRDIGID IIRAVGVDTG GCNIQFAVDP SNGRIIVIEM NPRVSRSSAL ASKATGFPIA KIAAKLALGY RLDEIPNDIT KVTPASFEPT LDYVVVKVPR FNFEKFPAAD TTLTTTMKSV GEAMAIGRNY ATALQKALRS LEKRGSSFHW GDEPRTKDEL VEVSKTPTDG RIVVVQQALR AGASVPEMFE ATGIDPWFLD QIVLINEVAD FVRDAAKLDA ETILLAKDHG FSDAQLGQLR GIPEVEVRGI RHALSIRPVY KTVDTCAGEF PALTPYHYSS YDFETEVTPS DRQKIVIIGS GPNRIGQGVE FDYSCVHASF ALSDAGYETI MVNCNPETVS TDYDTSDRLY FEPLTLEDVL EVLYAEAASG EIFGVVCQLG GQTPLGLAKG IEEAGYRILG TSPAAIDLAE ERQLFSEILD TAGLVAPRHG TATDAEGAVA VAEDIGYPVL VRPSFVLGGR GMEIVYDTPS LYDYFVRTAG EVIIGPGMPL LVDRFLDDAV EIDVDALYDG TELYIGGVME HIEEAGIHSG DSACTLPPIS LGRSEIDRVR TATLAIAEGV GVRGLLNVQF AISAGILYVI EANPRASRTV PFVSKALGIP LAKAAARIMS GSTIDELKTE GLLPPSDGSR VPLDSPVSVK EAVLPFKRFR TKDGQTVDSV LGPEMRSTGE VMGIDKDFPT AFAKSQAAAY GGMPLSGTVF ISVADSDKRA VILPAHRLQE LGFTLVATEG TAEILARNGI NVRIVNKYSE TQASGARNIV DLINDGEIDI IVNTPSGRSA RADGYEIRAA AVAADKALFT TIAVLGAAVS AMDAVRQGFD VRSLQEYAAD RAARG //