UniProt: S0JIU4

Database: UniProt
Entry: S0JIU4_9FIRM

LinkDB:  S0JIU4_9FIRM 
Original site:  S0JIU4_9FIRM

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Ontology (5)   
   GO (5)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (21)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (5)   
   SMART (2)   
All databases (28)   

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ID   S0JIU4_9FIRM            Unreviewed;      1072 AA.
AC   S0JIU4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EOT27798.1};
GN   ORFNames=C805_01906 {ECO:0000313|EMBL:EOT27798.1};
OS   Eubacterium sp. 14-2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=1235790 {ECO:0000313|EMBL:EOT27798.1, ECO:0000313|Proteomes:UP000014176};
RN   [1] {ECO:0000313|EMBL:EOT27798.1, ECO:0000313|Proteomes:UP000014176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14-2 {ECO:0000313|EMBL:EOT27798.1,
RC   ECO:0000313|Proteomes:UP000014176};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Eubacterium bacterium 14-2.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC         phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC         ChEBI:CHEBI:456216; EC=6.3.4.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00043687};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC   -!- SIMILARITY: Belongs to the CarB family.
CC       {ECO:0000256|ARBA:ARBA00009799}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOT27798.1}.
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DR   EMBL; ASSS01000005; EOT27798.1; -; Genomic_DNA.
DR   RefSeq; WP_016214937.1; NZ_KE159567.1.
DR   AlphaFoldDB; S0JIU4; -.
DR   STRING; 1235790.C805_01906; -.
DR   PATRIC; fig|1235790.3.peg.2047; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_0_9; -.
DR   OrthoDB; 9804197at2; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000014176; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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:0006520; P:amino acid metabolic process; IEA:UniProt.
DR   CDD; cd01424; MGS_CPS_II; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 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   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
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; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51855; MGS; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014176};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          133..327
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   DOMAIN          933..1072
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   1072 AA;  117712 MW;  2AAFE1D196F6DB96 CRC64;
     MSQRKDIHKV LIIGSGPIVI GQACEFDYSG TQACKALRSL GYEIVLVNSN PATIMTDPET
     ADVTYIEPLN AERMEQIIAK ERPDALLPNL GGQSGLNLCS ELAKTGVLDK YNVQVIGVQV
     DAIERGEDRI EFKKTMDSLG IEMARSEVAY SVEEAMEIAD KLGYPVVLRP AYTMGGAGGG
     LVYNVEELKT VCARGLQASL VGQVLVEESI LGWEELELEV VRDADNNMIT VCFIENIDPL
     GVHTGDSFCS APMLTISEEV QKRLQEKSYK IVESIQVIGG TNVQWAHDPK TDRDIVIEIN
     PRTSRSSALA SKATGFPIAL VSAMLATGLT LSDIPCGKYG TLDKYVPDGD YVVIKFARWA
     FEKFKGVEDK LGTQMRAVGE VMSIGKTFKE AFQKAIRSLE TGRYGLGHAR DFDKKSKEDL
     LKLLITPSSE RYFIIYEALR KGATPEEIHE ITKVKHYFLE QMKELAEEEE ALAAEKGCLP
     SDHALINAKK HGFSDKYLSQ ILEIPEADIR EKRISLGVEE AWEGVHVSGT KDNAYYYSTY
     NAEDKNPVSE GKPKIMILGG GPNRIGQGIE FDYCCVHASL ALKKLGFETI IVNCNPETVS
     TDYDTSDKLY FEPLTLEDVL SIYKKEKPAG VIAQFGGQTP LNLAADLEKN GVKILGTAPS
     VIDLAEDRDL FRAMMDKLEI PMPESGMAVN VEEALHIAEK IGYPVMVRPS YVLGGRGMEV
     VYDADSMEGY MNAAVGVTPD RPILIDRFLG HATECEADAI SDGTHAFVPA VMEHIELAGV
     HSGDSACIIP SRHISEENVA TIKEYTRKIA EEMHVQGLMN MQYAIENGKV FVLEANPRAS
     RTVPLVSKVC NIRMVPLAID IVTAELTGNS SPVPELKETK TGYYGVKESV FPFNMFQEVD
     PVLGPEMRST GEVLGLSESY GEAFFKAQEA AQMKLPLEGT VLISVSDRDK PEVVDIAGKF
     AEAGFHIIAS KNTCRLIREA GIEADMVHKL QEGRPNMLDL ITNGKIDLII NTPIGQERKT
     DDSYLRKAAI KKKIPYMTTM AAAKATVSGI LSLKKHGSSE VRSLQQLHGN MK
//

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