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 01-MAY-2013, entry version 55.
DE RecName: Full=Carbamoyl-phosphate synthase large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=carB; 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 -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC carbamoyl phosphate from bicarbonate: step 1/1.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
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 (By
CC similarity).
CC -!- SIMILARITY: Belongs to the CarB family.
CC -!- SIMILARITY: Contains 2 ATP-grasp domains.
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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; PMANLAT; -.
DR ProtClustDB; PRK05294; -.
DR BioCyc; MSP189918:GH4X-2471-MONOMER; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA: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; CarbamoylP_synth_lsu_oligo; 1.
DR SUPFAM; SSF52335; MGS-like_dom; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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; Repeat.
FT CHAIN 1 1112 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_1000066370.
FT DOMAIN 138 333 ATP-grasp 1.
FT DOMAIN 693 884 ATP-grasp 2.
FT NP_BIND 164 221 ATP (By similarity).
FT NP_BIND 719 776 ATP (By similarity).
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 (By similarity).
FT METAL 304 304 Magnesium or manganese 1 (By similarity).
FT METAL 304 304 Magnesium or manganese 2 (By similarity).
FT METAL 306 306 Magnesium or manganese 2 (By similarity).
FT METAL 843 843 Magnesium or manganese 3 (By similarity).
FT METAL 855 855 Magnesium or manganese 3 (By similarity).
FT METAL 855 855 Magnesium or manganese 4 (By similarity).
FT METAL 857 857 Magnesium or manganese 4 (By similarity).
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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