CARB_METLZ
ID CARB_METLZ Reviewed; 1053 AA.
AC A2SQ53;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Mlab_0283;
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z;
RX PubMed=21304657; DOI=10.4056/sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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}.
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DR EMBL; CP000559; ABN06459.1; -; Genomic_DNA.
DR RefSeq; WP_011832660.1; NC_008942.1.
DR AlphaFoldDB; A2SQ53; -.
DR SMR; A2SQ53; -.
DR STRING; 410358.Mlab_0283; -.
DR EnsemblBacteria; ABN06459; ABN06459; Mlab_0283.
DR GeneID; 4795384; -.
DR KEGG; mla:Mlab_0283; -.
DR eggNOG; arCOG01594; Archaea.
DR HOGENOM; CLU_000513_1_2_2; -.
DR OMA; IEPAGIH; -.
DR OrthoDB; 911at2157; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000365; 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; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_01210_A; CPSase_L_chain_A; 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..1053
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_1000066365"
FT DOMAIN 131..323
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 661..852
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 918..1053
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..397
FT /note="Carboxyphosphate synthetic domain"
FT REGION 398..530
FT /note="Oligomerization domain"
FT REGION 531..919
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 920..1053
FT /note="Allosteric domain"
FT BINDING 157..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 294
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 687..744
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 811
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 823
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 823
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 825
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ SEQUENCE 1053 AA; 115992 MW; DE7E38822556307A CRC64;
MPKNTSLKKV LLIGSGPIQI GQAAEFDYAG SQACKAVREE GIEVVLVNSN PATIQTDPET
ADKVYVEPLK ADIIAEIIKK EKPDGILSGM GGQTGLNLTA ELYELGALEG VQILGTPLEA
IYHGEDRDLF KKLMLEIGEP IPKSFILTKI EQLDEAYEEV GLPAIIRPAY TLGGAGGGVA
NTKEELRTIV EHGLTKSRVH QVLIEESVKG WNEIEFEVMR DAADTCIIIC GMENVDPMGV
HTGESVVVAP ILSLTSDEFG IMRRAAIKII RALNVQGGCN IQFAFNNGDY RVIEVNPRVS
RSSALASKAT GYPIARVAAK VAIGLHLDEI MNTVTGCTPA CFEPAVDYVV VKVSRWPFDK
FKTADRTLTT SMKSTGEVMA IGRTVEEGFK KALRSLDTDI YRHTDLNEIR MILSRPTDER
FPTLFDAFRL GMTVKEVYDL TQIEPFFLEK IQNVVDIELE LRDHPTEELV KTSKKFGFSN
AEIRELTGWN IYKIESLVGL PTYKMVDTCS AEFPAKTPYY YSTWEQECEL TQSDRKKILI
LGSGAIRIGQ GIEFDYCTVH AVKSLREEGI EVHILNNNPE TVSTDFDTSD RLYFEPMQLE
DVVNILRKGD YDGVMVQFGG QNSVNLAIPI QEEIKLFGLK TKVLGTSPDN MDVAEDRNRF
SVLLDQNNIP SPANGSAYSE KEAYAIANKI GYPVLVRPSY VLGGRAMELV HDELELQTYI
KEAVRVSNTH PVLIDRYLDN ATELDVDAVS DGETVLIGGV MEHIEEAGVH SGDSACVIPT
QTLTPEQIAT VKDYTRKIAL SLGVVGLINI QYAIHKGTVY VLEANPRASR TVPFVSKATG
LPLAKIAAKL MLGKKLADLG YQEKEISHVA VKEVLLPFSR LPGVDPILGP EMKSTGEVIG
IDYDFGRAFY KASQAADNTI PLKGNVFISV TNDQKTEILP IARKLYDLGF SLYGTEGTVK
FLAQNDIPMN LVRKVQEGSP NILDMIRALD VHLLINTPGD KNARADHLQI MRASIDYSIP
YITTIFGAEA AVQAIESMKT NTITVEPLSH YHS
