(data stored in SCRATCH zone)

HOGENOM: FUNUC1_1_PE1002

ID   FUNUC1_1_PE1002                      STANDARD;      PRT;   1058 AA.
AC   FUNUC1_1_PE1002; Q8RG86;
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   (FUNUC1_1.PE1002).
GN   Name=carB; OrderedLocusNames=FN0422;
OS   FUSOBACTERIUM NUCLEATUM SUBSP. NUCLEATUM ATCC 25586.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FUNUC1_1.PE1002.
CC       Fusobacterium nucleatum subsp. nucleatum ATCC 25586 chromosome, complet
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:CARB_FUSNN
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=AAL94625.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000234582 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8RG86; -.
DR   EMBL; AE009951; AAL94625.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_603326.2; NC_003454.1.
DR   ProteinModelPortal; Q8RG86; -.
DR   GeneID; 991870; -.
DR   GenomeReviews; AE009951_GR; FN0422.
DR   KEGG; fnu:FN0422; -.
DR   NMPDR; fig|190304.1.peg.1005; -.
DR   OMA; QGVTKEI; -.
DR   ProtClustDB; PRK05294; -.
DR   BioCyc; FNUC190304:FN0422-MON; -.
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_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; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   HOGENOMDNA; FUNUC1_1.PE1002; -.
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.
SQ   SEQUENCE   1058 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPKRKDIKTI LVIGSGPIII GQAAEFDYAG TQACLSLREE GYEVILVNSN PATIMTDKEI
     ADKVYIEPLT VEFLSKIIRK EKPDALLPTL GGQVALNLAV SLHESGILDE CGVEILGTKL
     TSIKQAEDRE LFRDLMNELN EPVPDSAIVH TLEEAENFVK EIDYPVIVRP AFTMGGTGGG
     ICYNEEDLHE IVPNGLNYSP VHQCLLEKSI AGYKEIEYEV MRDSNDTAIV VCNMENIDPV
     GIHTGDSIVV APSQTLTDRE HHMLRDVSLK IIRALKIEGG CNVQIALDPN SFKYYIIEVN
     PRVSRSSALA SKATGYPIAK IAAKIAVGMT LDEIINPVTK SSYACFEPAI DYVVTKIPRF
     PFDKFGDGDR YLGTQMKATG EVMAIGRTLE ESLLKAIRSL EYGVHHLGLP NGEEFSLEKI
     IKRIKLAGDE RLFFIGEALR RDVSIEEIHE YTKIDLFFLN KMKNIIDLEH LLKDNKGNIE
     LLRKVKTFGF SDRVIAHRWE MTEPEITELR HKHNIRPVYK MVDTCAAEFD SNTPYFYSTY
     EFENESTRSD KEKIVVLGSG PIRIGQGIEF DYATVHAIMA IKKLGYEAIV INNNPETVST
     DFSISDKLYF EPLTQEDVME ILDLEKPLGV VVQFGGQTAI NLADKLVKNG IQILGSSLDS
     IDTAEDRDRF EKLLIGLKIP QPLGKTAFDV ETALKNANEI GYPVLVRPSY VLGGRAMEIV
     YNDEDLTKYM EKAVHINPDH PVLIDRYLIG KEIEVDAISD GENTFIPGIM EHIERAGVHS
     GDSISIYPPQ SLSEKEIETL IDYTKKLASG LEVKGLINIQ YVVSKGEIYV LEVNPRASRT
     VPFLSKVTGV PVANIAMQCI LGKKLKDLGF TKDIADIGNF VSVKVPVFSF QKLKNVDTTL
     GPEMKSTGEV IGTDVNLQKA LYKGLTAAGI KIKDYGRVLF TIDDKNKEAA LNLAKGFSDV
     GFSILTTEGT GIYFEEYGLK VKKVGKIDNS DYSVLDAIQN GDVDIVINTT TKGKSSEKDG
     FRIRRKATEY GVICFTSLDT ANALLRVIES MSFRVQTL
//

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