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-APR-2013, entry version 99.
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 /
OS JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanobacteria; Methanobacteriales;
OC 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;
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.,
RA Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum
RT deltaH: functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB85494.1; Type=Frameshift; Positions=230; Note=Produces two separate ORFs;
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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 RefSeq; NP_276131.1; NC_000916.1.
DR RefSeq; NP_276132.1; NC_000916.1.
DR ProteinModelPortal; O27077; -.
DR STRING; 187420.MTH996; -.
DR EnsemblBacteria; AAB85493; AAB85493; MTH_996.
DR EnsemblBacteria; AAB85494; AAB85494; MTH_997.
DR GeneID; 1471404; -.
DR GeneID; 1471405; -.
DR KEGG; mth:MTH996; -.
DR KEGG; mth:MTH997; -.
DR eggNOG; COG0458; -.
DR KO; K01955; -.
DR ProtClustDB; CLSK420531; -.
DR BioCyc; MTHE187420:GJNM-998-MONOMER; -.
DR BioCyc; MTHE187420:GJNM-999-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_A; CPSase_L_chain_A; 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; 2.
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; Reference proteome;
KW Repeat.
FT CHAIN 1 1060 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_0000145080.
FT DOMAIN 131 326 ATP-grasp 1.
FT DOMAIN 664 858 ATP-grasp 2.
FT NP_BIND 157 214 ATP (By similarity).
FT NP_BIND 690 747 ATP (By similarity).
FT REGION 1 400 Carboxyphosphate synthetic domain.
FT REGION 401 539 Oligomerization domain.
FT REGION 540 926 Carbamoyl phosphate synthetic domain.
FT REGION 927 1060 Allosteric domain.
FT METAL 283 283 Magnesium or manganese 1 (By similarity).
FT METAL 297 297 Magnesium or manganese 1 (By similarity).
FT METAL 297 297 Magnesium or manganese 2 (By similarity).
FT METAL 299 299 Magnesium or manganese 2 (By similarity).
FT METAL 814 814 Magnesium or manganese 3 (By similarity).
FT METAL 829 829 Magnesium or manganese 3 (By similarity).
FT METAL 829 829 Magnesium or manganese 4 (By similarity).
FT METAL 831 831 Magnesium or manganese 4 (By similarity).
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
//
