CARB_MYCTU
ID CARB_MYCTU Reviewed; 1115 AA.
AC P9WPK3; L0T9H0; P57689;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
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}; OrderedLocusNames=Rv1384;
GN ORFNames=MTCY02B12.18, MTCY21B4.01;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; Evidence={ECO:0000255|HAMAP-
CC 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; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01210}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
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; AL123456; CCP44143.1; -; Genomic_DNA.
DR PIR; A70990; A70990.
DR RefSeq; WP_003898855.1; NZ_NVQJ01000050.1.
DR RefSeq; YP_177804.1; NC_000962.3.
DR AlphaFoldDB; P9WPK3; -.
DR SMR; P9WPK3; -.
DR STRING; 83332.Rv1384; -.
DR PaxDb; P9WPK3; -.
DR GeneID; 886253; -.
DR KEGG; mtu:Rv1384; -.
DR TubercuList; Rv1384; -.
DR eggNOG; COG0458; Bacteria.
DR OMA; IEPAGIH; -.
DR PhylomeDB; P9WPK3; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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 GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR CDD; cd01424; MGS_CPS_II; 1.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 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; IPR013815; ATP_grasp_subdomain_1.
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; 2.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..1115
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145023"
FT DOMAIN 138..333
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 693..884
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 966..1113
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..407
FT /note="Carboxyphosphate synthetic domain"
FT REGION 408..559
FT /note="Oligomerization domain"
FT REGION 560..965
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 966..1115
FT /note="Allosteric domain"
FT BINDING 164..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 719..776
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 843
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 855
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 855
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 857
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ SEQUENCE 1115 AA; 118961 MW; 293F6A35FDE05981 CRC64;
MPRRTDLHHV LVIGSGPIVI GQACEFDYSG TQACRVLRAE GLQVSLVNSN PATIMTDPEF
ADHTYVEPIT PAFVERVIAQ QAERGNKIDA LLATLGGQTA LNTAVALYES GVLEKYGVEL
IGADFDAIQR GEDRQRFKDI VAKAGGESAR SRVCFTMAEV RETVAELGLP VVVRPSFTMG
GLGSGIAYST DEVDRMAGAG LAASPSANVL IEESIYGWKE FELELMRDGH DNVVVVCSIE
NVDPMGVHTG DSVTVAPAMT LTDREYQRMR DLGIAILREV GVDTGGCNIQ FAVNPRDGRL
IVIEMNPRVS RSSALASKAT GFPIAKIAAK LAIGYTLDEI VNDITGETPA CFEPTLDYVV
VKAPRFAFEK FPGADPTLTT TMKSVGEAMS LGRNFVEALG KVMRSLETTR AGFWTAPDPD
GGIEEALTRL RTPAEGRLYD IELALRLGAT VERVAEASGV DPWFIAQINE LVNLRNELVA
APVLNAELLR RAKHSGLSDH QIASLRPELA GEAGVRSLRV RLGIHPVYKT VDTCAAEFEA
QTPYHYSSYE LDPAAETEVA PQTERPKVLI LGSGPNRIGQ GIEFDYSCVH AATTLSQAGF
ETVMVNCNPE TVSTDYDTAD RLYFEPLTFE DVLEVYHAEM ESGSGGPGVA GVIVQLGGQT
PLGLAHRLAD AGVPIVGTPP EAIDLAEDRG AFGDLLSAAG LPAPKYGTAT TFAQARRIAE
EIGYPVLVRP SYVLGGRGME IVYDEETLQG YITRATQLSP EHPVLVDRFL EDAVEIDVDA
LCDGAEVYIG GIMEHIEEAG IHSGDSACAL PPVTLGRSDI AKVRKATEAI AHGIGVVGLL
NVQYALKDDV LYVLEANPRA SRTVPFVSKA TAVPLAKACA RIMLGATIAQ LRAEGLLAVT
GDGAHAARNA PIAVKEAVLP FHRFRRADGA AIDSLLGPEM KSTGEVMGID RDFGSAFAKS
QTAAYGSLPA QGTVFVSVAN RDKRSLVFPV KRLADLGFRV LATEGTAEML RRNGIPCDDV
RKHFEPAQPG RPTMSAVDAI RAGEVNMVIN TPYGNSGPRI DGYEIRSAAV AGNIPCITTV
QGASAAVQGI EAGIRGDIGV RSLQELHRVI GGVER
