CARB_MYCLE
ID CARB_MYCLE Reviewed; 1121 AA.
AC Q9CCR2;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
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=ML0536;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAC30044.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL583918; CAC30044.1; ALT_INIT; Genomic_DNA.
DR PIR; H86975; H86975.
DR RefSeq; NP_301455.2; NC_002677.1.
DR RefSeq; WP_010907779.1; NC_002677.1.
DR AlphaFoldDB; Q9CCR2; -.
DR SMR; Q9CCR2; -.
DR STRING; 272631.ML0536; -.
DR PRIDE; Q9CCR2; -.
DR EnsemblBacteria; CAC30044; CAC30044; CAC30044.
DR KEGG; mle:ML0536; -.
DR PATRIC; fig|272631.5.peg.937; -.
DR Leproma; ML0536; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_11; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000806; Chromosome.
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; 3.30.1490.20; -; 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 3: Inferred from homology;
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..1121
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145022"
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..1121
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 1121 AA; 120017 MW; 2EABCB0A8D4281CD CRC64;
MPRRTDLNHV LVIGSGPIVI GQACEFDYAG TQACRVLRAE GLQVSLVNSN PATIMTDPEF
ADHTYVEPIT PAFVERVIVQ QAERGNRIDA LLATLGGQTA LNTAVALYEN GVLERYGVEL
IGADFEAIQR GEDRQRFKDL VAKVGGESAR SKVCFTMDEV RETVEDLGLP VVVRPSFTMG
GLGSGMAHSD EEVGRMAGAG LVASPSANVL IEESVYGWKE FELELMRDGH DSVVVVCSIE
NVDPMGVHTG DSVTVAPAMT LTDWEYQRMR DLGIAILREV GVDTGGCNIQ FAINPHDGRL
IVIEMNPRVS RSSALASKAT GFPIAKIAVK LAVGYTLDEI LNDITKETPA CFEPALDYVV
VKAPRFAFEK FPGADPTLTT TMKSVGEAMS LGRNFVEALG KVMRSLETGR FGFWTAPDPQ
GDVDQVLLRL KTPTEGRLYD VELALRLGAS TEKVAQVSGI DPWFVAQIGE LVKLRDELVA
APVLDAELLR RAKHNGLSDR QITALRPELL GEDGVRSLRK RLGIHPVYKT VDTCAAEFEA
KTPYHYSSYE LDPAAETEVV PQTEKPKVLI LGSGPNRIGQ GIEFDYSCVH AAITLSHNGF
ETVMVNCNPE TVSTDYDTAD RLYFEPLTFE DVLEVFYAEE QSAAGGAGVA GVIVQLGGQT
PLGLAQRLAD AGVPIVGTSP EAIDLAEDRG AFGDVLTAAG LPAPKYGTAT TFAQARRIAA
EIGYPVLVRP SYVLGGRGME IVYDEETLKD YITRATALSH EHPVLVDRFL EDAVEIDVDA
LCDGTEVYIG GVMEHIEEAG IHSGDSACAL PPVTLGRSDL EKVRQATEAI ARGIGVVGLL
NVQYALKEDV LYVLEANPRA SRTVPFVSKA TAIPLAKACA RIMLGSSISQ LRFEGMLAAS
GDGGNVASHA PIAVKEAVLP FNRLRRADGA AIDSLLGPEM KSTGEVMGID HDFGRAFAKS
QTAAYGSLPT QGTVFVSVAN RDKRLLVFPV KRLADLGFHV IATEGTAEML RRKGIPCDEV
RKHFEPPKAG RPALSAVDAI RAGDVDMVIN TPYGNSGPRI DGYEIRSAAV SVNIPCVTTV
QGASAAVQGI EAGIRGDIGV RSLQELHSAI GAGIAADNEV Q
