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Database: UniProt
Entry: A1UFK4
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ID   CARB_MYCSK              Reviewed;        1112 AA.
AC   A1UFK4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   26-NOV-2014, entry version 62.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000255|HAMAP-Rule:MF_01210};
GN   OrderedLocusNames=Mkms_2414;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Miller C.D., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) 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:0000255|HAMAP-Rule:MF_01210}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000255|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
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
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DR   EMBL; CP000518; ABL91612.1; -; Genomic_DNA.
DR   RefSeq; YP_938402.1; NC_008705.1.
DR   ProteinModelPortal; A1UFK4; -.
DR   STRING; 189918.Mkms_2414; -.
DR   PRIDE; A1UFK4; -.
DR   EnsemblBacteria; ABL91612; ABL91612; Mkms_2414.
DR   GeneID; 4613237; -.
DR   KEGG; mkm:Mkms_2414; -.
DR   PATRIC; 18103771; VBIMycSp70743_2923.
DR   eggNOG; COG0458; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; ARSAICH; -.
DR   OrthoDB; EOG6J1DC6; -.
DR   BioCyc; MSP189918:GH4X-2431-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.30.1490.20; -; 2.
DR   Gene3D; 3.30.470.20; -; 2.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
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; IPR016185; PreATP-grasp_dom.
DR   Pfam; PF00289; CPSase_L_chain; 2.
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; 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1112       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000066370.
FT   DOMAIN      138    333       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      693    884       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   NP_BIND     164    221       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     719    776       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    407       Carboxyphosphate synthetic domain.
FT   REGION      408    559       Oligomerization domain.
FT   REGION      560    965       Carbamoyl phosphate synthetic domain.
FT   REGION      966   1112       Allosteric domain.
FT   METAL       290    290       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       304    304       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       304    304       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       306    306       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       843    843       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       855    855       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       855    855       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       857    857       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1112 AA;  118976 MW;  D30EF5DD52EAC9C7 CRC64;
     MPRRTDLRHV LVIGSGPILI GQAAEFDYSG TQACRVLRAE GLTVTLINSN PATIMTDPEY
     ADYTYVEPIT PDFVERVIAQ QAERGNKIDA LLATLGGQTA LNTAVALSEN GVLERYDVEL
     IGADFDAIQR GEDRQRFKDI VTKVGGESAK SRVCFTMEEV RETVGELGLP VVVRPSFTMG
     GLGSGMAYSA EDVERMAGHG LASSPSANVL IEESIFGWKE YELELMRDRH DNVVVVCSIE
     NFDPMGVHTG DSVTVAPAMT LTDREYQTMR DLGIAILREV GVATGGCNIQ FAVNPKDGRL
     IVIEMNPRVS RSSALASKAT GFPIAKIAAK LAIGYTLDEI LNDITKETPA CFEPTLDYVV
     VKAPRFAFEK FPGADATLTT TMKSVGEAMS LGRNFIEALG KVMRSLETGR AGFWTAPDPI
     ATVDEVLENL RTPTDGRLYD IEFALRLGAS VEQVAEASGV DPWFVDQIAG LVALRTELLD
     APVLDGTLLR RAKNSGLSDR QIAALRPELA GEVGVRALRQ RLGIHPVFKT VDTCAAEFEA
     KTPYHYSSYE LDPAAESEVA PQAERPKVLI LGSGPNRIGQ GIEFDYSCVH AATTLSEAGF
     ETVMINCNPE TVSTDYDTAD RLYFEPLTFE DVLEIYYAES ASGAGGPGVA GVIVQLGGQT
     PLGLAERLEQ AGVPIVGTSP KAIDLAEDRG AFGEVLRTAG LPAPRFGLAT TFDQARRIAA
     DIGYPVLVRP SYVLGGRGME IVYDEQTLEG YITRATQLSP EHPVLVDRFL EDAIEIDVDA
     LCDGTEVYIG GIMEHIEEAG IHSGDSACAL PPVTLGRSDI ESVRRATEAI AHGVGVVGLL
     NVQYALKDDV LYVLEANPRA SRTVPFVSKA TAVPLAKACA RIMLGASIAQ LREEGVLAAT
     GDGATTARNA PVAVKEAVLP FHRFRKADGA QIDSLLGPEM KSTGEVMGID HDFGSAFAKS
     QTAAYGSLPS EGTVFVSVAN RDKRSLVFPV KRLADLGFKV LATEGTAEML RRNGIPCDEV
     RKHFEEPGAG RPARSAVEAI RAGDVAMVIN TPYGNSGPRI DGYEIRSAAV SMNIPCITTV
     QGASAAVQGI EASLRGDIGV MSLQELHSEL GN
//
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