UniProt: K4L4Y0

Database: UniProt
Entry: K4L4Y0_9FIRM

LinkDB:  K4L4Y0_9FIRM 
Original site:  K4L4Y0_9FIRM

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (21)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (5)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (31)   

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ID   K4L4Y0_9FIRM            Unreviewed;      1074 AA.
AC   K4L4Y0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:AFV06327.1};
DE            EC=6.3.5.5 {ECO:0000313|EMBL:AFV06327.1};
GN   ORFNames=DCF50_p2324 {ECO:0000313|EMBL:AFV06327.1};
OS   Dehalobacter sp. CF.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Dehalobacter.
OX   NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV06327.1, ECO:0000313|Proteomes:UP000000482};
RN   [1] {ECO:0000313|EMBL:AFV06327.1, ECO:0000313|Proteomes:UP000000482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF {ECO:0000313|EMBL:AFV06327.1};
RX   PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA   Tang S., Gong Y., Edwards E.A.;
RT   "Semi-automatic in silico gap closure enabled de novo assembly of two
RT   dehalobacter genomes from metagenomic data.";
RL   PLoS ONE 7:E52038-E52038(2012).
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}.
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DR   EMBL; CP003870; AFV06327.1; -; Genomic_DNA.
DR   RefSeq; WP_015044361.1; NC_018867.1.
DR   AlphaFoldDB; K4L4Y0; -.
DR   STRING; 1131462.DCF50_p2324; -.
DR   KEGG; dec:DCF50_p2324; -.
DR   PATRIC; fig|1131462.4.peg.2342; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_0_9; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000482; Chromosome.
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; 2.
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};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AFV06327.1};
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:UP000000482};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          133..327
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          671..862
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          932..1074
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   1074 AA;  117591 MW;  FCACB3C9F20670FF CRC64;
     MPKRTDINKI LIIGSGPIVI GQACEFDYSG TQACKALRKL GYKIVLVNSN PATIMTDPGI
     ADITYIEPLN LESLTKIIAK ERPDALLPNL GGQSALNLSS ELHQAGVLTK YNVKVIGVQL
     DAIERGEDRI AFKETMNRLG IEMPLSKAAY SVEEAEAIAQ ELGYPVVIRP AYTMGGTGGG
     LVYNAEELNV IASRGIAASL VGQILVEESV LGWEELELEV IRDAKNQMIT VCFIENIDAI
     GVHTGDSFCS APMLTISPEL QERLQKYSYS VVEAIEVIGG TNVQFAHDPK TGRVVIIEIN
     PRTSRSSALA SKATGLPIAL ISSMLAAGLT LDEIPYWRDG SLDKYTPSGD YVVIKFARWA
     FEKFPGSVDK LGTQMRAVGE VMSIGKNYKE AVQKSIRSLE TNRYGLGFAK DFHQRSLEEL
     MAMLAEPTSE RQFILYEALR KGADINDLYA LTYIKPYFLQ QMKELVLLEE EILKYSGQKL
     PDELLTQAKK DGFADRYLAM LLNLSEAEIR KQRAALGVVE GWEAVPVSGV EDAYYYFSTY
     NAPDKTTSSN QPKVMILGGG PNRIGQGIEF DYCCVHTAFA LRDLGYETVI VNCNPETVST
     DYDTSDKLYF EPLTVEDVLS IYEKEKPLGV IVQFGGQTPL NIADELKKAG VKILGTTPET
     IALAEDRDLF RKMMEKLDIP MPESGMAVNL EEALVIADRI GYPLMVRPSF VLGGRGMEVV
     HDAEMLSRYM AAAVGVTPDR PILIDRFLSN AIEAEADAIA DGKDAFVPTV MEHIELAGIH
     SGDSACVIPP INIPEKHLAT IVEYTKKIAQ EMNVIGLMNM QYAIADDKVY VLEANPRASR
     TVPLVSKVCN ISMARIATEI LMAVNDGKET SVKNLTSKIV PYFGVKEAVF PFNMFTEVDP
     VLGPEMRSTG EVLGLADSFG LAYYKAQEAT KSPLPESGTV LISVNDDDKP AALEIARNFA
     QIGFKIMATE GTHKFLLVNG IEAEKIKKLY EGRPNIVDSI TNKEIHLVIN SPSGKRSKHE
     DAYIRKAAIK YKVPYITTMT AAAASAKGIA AYDANGASGI TLKSLQEYHA EIKG
//

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