(data stored in ACNUC7421 zone)

HOGENOM: MEMAR1_1_PE1013

ID   MEMAR1_1_PE1013                      STANDARD;      PRT;   1081 AA.
AC   MEMAR1_1_PE1013; Q6LYH8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Carbamoyl-phosphate synthase large chain; EC=6.3.5
DE   5;AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
DE   (MEMAR1_1.PE1013).
GN   Name=carB; OrderedLocusNames=MMP1013;
OS   METHANOCOCCUS MARIPALUDIS S2.
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales; Methanococcaceae;
OC   Methanococcus.
OX   NCBI_TaxID=267377;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MEMAR1_1.PE1013.
CC       Methanococcus maripaludis S2 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:Q6LYH8_METMP
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   -!- GENE_FAMILY: HOG000234583 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q6LYH8; -.
DR   EMBL; BX950229; CAF30569.1; -; Genomic_DNA.
DR   RefSeq; NP_988133.1; NC_005791.1.
DR   HSSP; P00968; 1A9X.
DR   ProteinModelPortal; Q6LYH8; -.
DR   GeneID; 2761525; -.
DR   GenomeReviews; BX950229_GR; MMP1013.
DR   KEGG; mmp:MMP1013; -.
DR   NMPDR; fig|267377.1.peg.1013; -.
DR   OMA; QGVTKEI; -.
DR   ProtClustDB; CLSK926298; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005479; CarbamoylP_synth_lsu_ATP-bd.
DR   InterPro; IPR005483; CarbamoylP_synth_lsu_CPS-dom.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   InterPro; IPR016185; PreATP-grasp-like.
DR   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 2.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
DR   Gene3D; G3DSA:1.10.1030.10; CarbamoylP_synth_lsu_oligo; 1.
DR   Gene3D; G3DSA:3.40.50.1380; MGS-like_dom; 1.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 2.
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; 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; PS00867; CPSASE_2; 2.
DR   HOGENOMDNA; MEMAR1_1.PE1013; -.
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
SQ   SEQUENCE   1081 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKREDIKKVM ILGSGPIVIG QAAEFDFSGS QACKSLKEEG IYTILVNSNP ATIQTDTNIA
     DKVYLEPLNP KILEKIIEKE QPDAILPTMG GQTGLNLAME LSKRGILEKH GVELLGSTES
     VIETSEDRDL FNKAMEEINQ PIAKSAAVHS VEEAIGATKE LGYPAIVRPA FTLGGTGGGI
     ANNEEELIEI TKKGLKYSMI KQVLIDQSLL GWKEYEYEVM RDKNDTCIVV CNMENIDPMG
     IHTGESIVTA PSQTLSDEFH QKLRDASLQI IRHLKIEGGC NVQFAVNPEM TDYVVIEVNP
     RVSRSSALAS KATGYPIAKI AAKIAIGRTL DEIQNDVTKE TPASFEPTID YVVVKIPRWP
     FDKFRTVDKK LGTSMKSTGE IMAIGRNLEE ALQKAVRSLD IGRFGIIADG KDKEYSNSEI
     VDILEHATDE RLFVIAYALD KGWSVDGICE RTGINPFFIE KIKKIIDCKK ELEVISRIPV
     DDEKLKEILL KAKSLGFSDV QISKIFSKTE NEIRDLRKRL EVIPVYKMVD TCAAEFEAKT
     PYYYSAYERY FDEEQNESVS SDRKKVIILG SGPIRIGQGV EFDYSTVHAI FALKELGIEA
     IIVNNNPETV STDYDTSDKL YFEPLVYEEI MNIIENENKN GQLLGVIVQF GGQTAINLAM
     KLYNSGVNIL GTSPQSIDLA EDRDQFIHVL EKLKIPQADG ATAFSEEQAL KVVERIGYPA
     LVRPSYVLGG RAMQIVYNTE DLKDYMREAV KVSSDHPILI DKFLEEAVEV DVDAVCDGES
     VFIGAIMEHI EEAGIHSGDS ACVIPPQTLS KEVIEKIAEH TTKLALELGV IGLLNIQYAV
     KDGVVYIIEA NPRASRTIPY VSKSVGVPLA KIATNAIMGK KLKEMGYFGL AKSKYVSVKE
     AVFPFLKLPG VDPVLSPEMK STGEAIGIDQ DFGKAFYKSQ LSANMELPTS GTVFISVRNR
     DKDNITKIAK KYHNLGFEIV ATRGTARELR LFDIPVREVR KISESMQNSV LDLMQKGEVD
     LIINTSSGDK AKTDGYFIRR AAVELNIPCM TTLQGAYAAI KAIEAIKSGE LGVYSLNELE
     N
//

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