(data stored in SCRATCH zone)

SWISSPROT: D1YV00_METPS

ID   D1YV00_METPS            Unreviewed;      1084 AA.
AC   D1YV00;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 59.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000256|HAMAP-Rule:MF_01210,
GN   ECO:0000313|EMBL:BAI60272.1};
GN   OrderedLocusNames=MCP_0200 {ECO:0000313|EMBL:BAI60272.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60272.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(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:0000256|HAMAP-
CC         Rule:MF_01210};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01210}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01210}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01210}.
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DR   EMBL; AP011532; BAI60272.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0200; -.
DR   EnsemblBacteria; BAI60272; BAI60272; MCP_0200.
DR   KEGG; mpd:MCP_0200; -.
DR   PATRIC; fig|304371.9.peg.207; -.
DR   eggNOG; arCOG01594; Archaea.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234583; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001882; 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:InterPro.
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; 3.40.50.1380; -; 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; 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; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YV00.
DR   SWISS-2DPAGE; D1YV00.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|HAMAP-Rule:MF_01210};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE-
KW   ProRule:PRU00409};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   DOMAIN          133..325
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          672..863
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          1..399
FT                   /note="Carboxyphosphate synthetic domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   REGION          932..1084
FT                   /note="Allosteric domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1084 AA;  119608 MW;  7B9BE85CC42FC882 CRC64;
     MPKRTDVRKV LLIGSGPILI GQAAEFDFSG SQACRSLREE GIEVVLVNSN PATIMTDPEM
     ADAVYIEPIT PDVVAQIIER ERPDGILAGL GGQTGLNITS ELAEMGVLEK YGVKILGTPL
     KAIYDTEDRD RFKHAMESIG EKVPRSFACH TVDEAVAVID RLGLPLIIRS AFTLGGTGSG
     VAHTVQDVRH IAEIGLNKSR IHQILVEESV LGWKEFEYEV MRDASDTCIT ICNMENIDPM
     GIHTGESIVV TPSQTLSDAD HQTLRSAAIK IIRALGIEGG CNIQFAWNDG DYRIVEVNPR
     VSRSSALASK ATGYPIARTA AKIALGLRLD EIQNKVTMET PASFEPTIDY VVVKIPRWPF
     DKFKNADRHI TTSMKSTGEV MAIGRTYEEA YQKALNSLDI SEFWGYGNWS RAEMVDLLKN
     PTHERMFVIY KALQTGAFTI DQIAKLTNID PWFIKKLKNI VDMADALKAD IDPGLLRRAK
     RMGFTDEWIA ELRGTSPEAI SDMRHKYGII PTFKMVDTCA AEFAAKTPYY YSSYEQECEL
     TPSDRKKVLI IGAGPIRIGQ GIEFDYCTVH AVKALRESGI EAHIINNNPE TVSTDFDVSD
     KLFFEPITLE HVMNIIEKER PYGVMVQFGG QTSVNMAIPL QMELNRRKDL NTVIIGTSPD
     DMNIAEDRDL WGRMMKEMGI LQPEHGIAYS TDEAKVEAAR IGYPILVRPS YVLGGRAMEI
     VYDEADLERY MTEAVKVSRK HPVLIDDFLE DATEIDVDAI SDGKDVLIGA IMEHIEEAGI
     HSGDSACVIP PQSLSKEVQD QVRDITRKIA LALNVIGCVN IQMAYKDGKV YVLEANPRSS
     RTIPFVSKAT GLPLAKIAAK AIIGYSLKEM GYTEEPKPKY VSVKEVVLPF DKLPGADPLL
     GPEMRSTGEV MGIDTDFGKA FFKAEQSAFN SLPLEGTVFI SVRDEDKKEM ARLAKVLHAN
     GLKLIGTTGT KKYLEAQGIP VTLISKVHEG SPNVIDLMRR GKVDLIINTP TSKMARKDGS
     RIRRAAIDYD VPYLTTIQAV RASADAINAM GKRKMSILSL NEYLGHAAAP VPAVDAFKTR
     EPAA
//

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