CARB_METTH
ID CARB_METTH Reviewed; 1060 AA.
AC O27077; O27078;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=MTH_996/MTH_997;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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;
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.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (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 the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85494.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR EMBL; AE000666; AAB85493.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE000666; AAB85494.1; ALT_FRAME; Genomic_DNA.
DR PIR; D69233; D69233.
DR PIR; E69233; E69233.
DR AlphaFoldDB; O27077; -.
DR SMR; O27077; -.
DR STRING; 187420.MTH_996; -.
DR EnsemblBacteria; AAB85493; AAB85493; MTH_996.
DR EnsemblBacteria; AAB85494; AAB85494; MTH_997.
DR KEGG; mth:MTH_996; -.
DR KEGG; mth:MTH_997; -.
DR PATRIC; fig|187420.15.peg.979; -.
DR HOGENOM; CLU_000513_1_0_2; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000005223; 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_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; 2.
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..1060
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145080"
FT DOMAIN 131..326
FT /note="ATP-grasp 1"
FT DOMAIN 664..858
FT /note="ATP-grasp 2"
FT DOMAIN 925..1060
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..400
FT /note="Carboxyphosphate synthetic domain"
FT REGION 401..539
FT /note="Oligomerization domain"
FT REGION 540..926
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 927..1060
FT /note="Allosteric domain"
FT BINDING 157..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 690..747
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 814
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 829
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 829
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 831
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1060 AA; 116278 MW; 56716027BA1EDDCA CRC64;
MPRDESINKV LIIGSGPIQI GQAAEFDYSG SQACKSLREE GIETVLVNSN PATIQTDMEM
ADRVYVEPLT PEIVAKIIQK EKPDAVLPTM GGQTGLNVAT GLAEMGALEG VRVIGSSIET
IRNVEDRDLF DSFMKKLNEP VPAARAVSSV EEALEAVEEI GYPVIVRPAF TLGGTGGGVA
HSRDELIEIA TRGLEMSFIN QVLIDQSVLG WKEFEYEVMR DRNDTCIIVL CNMENIDPMG
IHTGESVVVA PAQTLSDEDN QRLRDAAIKI IRALKIEGGC NIQFAVHPET GEYKVIEVNP
RVSRSSALAS KATGYPIAKI AAKIAVGMTL DEIQNDITKE TPASFEPTID YVVTKIPRWP
FDKFKGISRE IGVQMKSTGE VMAIGRTLEE SLNKAIRSLD IGADGFTETP YTRADLENPT
DQRLFQVYTA LRDGMSIEEI HGLTQIDPFF LQKISNIAEF ESSITRESLE DPRILLKAKR
MGFSDSRLAS LTGMDESSIR ALRLENNIKP VYKMVDTCAA EFEARTPYYY GCYDLEDEVE
VSDRRKVLII GSGPIRIGQG IEFDYCCVHA AMALTEDGYE TIMVNNNPET VSTDYDISDK
LYFEPLTLED VLAIIEKEKP EGVVVQFGGQ TSINLAVPLA EAGVRILGTP HESIDRVEDR
ERFTEVLNKL GIPQAPYGIA KSFEDARAVA ERIGYPVLVR PSYVLGGRAM EIVYDDVELE
EYMREAVRVS PEHPILVDKF LEDAIEVDVD ALCDGTDVYI GGIMEHIEEA GVHSGDSACV
IPPQSIPEDI IDTIKEYTRK LALELEVVGL INIQYAVKPD SDPSVYILEA NPRASRTVPF
VSKATGVPLA KMAARLMMGA KLRDLGLTEE KDIEHVAVKE SVFPFIKLPG ADSVLGPEMK
STGEAMGIDE NFGIAYYKSQ LSASMDLLNE GKVFISVRDQ DKDKIADIVK KADELGFRIM
ATRGTARAVS DIADIEVVRK VSQGSPNIRD AILDGEVGLI INTPSGKQSA DDGYLIRRMA
VELGIPYVTT LAGARAALNA IEAVRMGKIT VKSLDEYHGM
