UniProt: K8EZ41

Database: UniProt
Entry: K8EZ41_9CHLO

LinkDB:  K8EZ41_9CHLO 
Original site:  K8EZ41_9CHLO

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Ontology (5)   
   GO (5)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (4)   
   SMART (2)   
All databases (29)   

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ID   K8EZ41_9CHLO            Unreviewed;      1219 AA.
AC   K8EZ41;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:CCO14498.1};
GN   ORFNames=Bathy01g05430 {ECO:0000313|EMBL:CCO14498.1};
OS   Bathycoccus prasinos.
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Bathycoccaceae; Bathycoccus.
OX   NCBI_TaxID=41875 {ECO:0000313|EMBL:CCO14498.1, ECO:0000313|Proteomes:UP000198341};
RN   [1] {ECO:0000313|EMBL:CCO14498.1, ECO:0000313|Proteomes:UP000198341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC 1105 {ECO:0000313|EMBL:CCO14498.1,
RC   ECO:0000313|Proteomes:UP000198341};
RA   Genoscope - CEA;
RL   Submitted (OCT-2011) 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}.
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DR   EMBL; FO082278; CCO14498.1; -; Genomic_DNA.
DR   RefSeq; XP_007515619.1; XM_007515557.1.
DR   AlphaFoldDB; K8EZ41; -.
DR   STRING; 41875.K8EZ41; -.
DR   GeneID; 19018278; -.
DR   KEGG; bpg:Bathy01g05430; -.
DR   eggNOG; KOG0370; Eukaryota.
DR   OrthoDB; 309at2759; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000198341; Chromosome_1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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   HAMAP; MF_01210_B; CPSase_L_chain_B; 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; 1.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51855; MGS; 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   Membrane {ECO:0000256|SAM:Phobius};
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:UP000198341};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        76..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          263..459
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          824..1017
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1084..1219
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   1219 AA;  132334 MW;  2B0B2DBFC05BAE27 CRC64;
     MQSQSVMSSA KPTNGTLFGS RHDVSAAALK KASTKAQQQQ SRRRLQPIDA VSAAGKEFRA
     WDDAKNSKKR TDLKKIMIIG AGPIVIGQVI TLSLLSVFVF FIDPPPVRSS GRRVGDDTMM
     MMSFKIVCLC FWFVFGSNFQ TTPTKIASVS RHACEFDYSG TQACKALRAE GYDVILINSN
     PATIMTDPET AARTFITPMT PEYVEKIIAA EKPDAVLPTM GGQTALNLTK ALAEAGIFEK
     YGVELIGAKL PAINKAEDRQ LFKDAMTKIG LKTPQSGTAE TWEQAKEIAA EIGTLPLIIR
     PAFTLGGSGG GIAYNMKEFE QITKGGLDAS ATSQVLIEQS LLGWKEYELE VMRDLADNVV
     IVCSIENFDP MGVHTGDSIT IAPAQTLTDK EYQRLRDASL AIIREIGVEC GGSNVQMAVN
     PADGELMIIE MNPRVSRSSA LASKATGFPI AKMAAKMALG ATMDGIPNDI TMKTPAAFEP
     SIDYVVTKIP RFAFEKFPGA EPILTTQMKS VGEAMAMGRT WQESFNKALR SLETGLSGWG
     LNKNDGFMQN DPELIKERLV VPSPERVVAL HEAFMSGMSE DEIIRLTTMD PWFIRQLGDL
     YQTECWLKSL SSMDDLSVED WTQVKRRGYS DAQICRAFPG TVEADVRQKR KSMGVVAAMK
     RVDTCAAEFE SDTPYMYSSY DGSCEAKPTN GRKILILGGG PNRIGQGIEF DYCCCHAAFA
     LSDAGYETIM LNSNPETVST DYDTSDRLYF EPLTVEDVLN VCEVERPEGI IVQFGGQTPL
     SLATKLEAAL KANPIQAASG NGVTHILGTP PDSIDAAEDR DRWMDILKEL DIRQPAGGVC
     VDEGEALSTA ERVGYPVMVR PSYVLGGRAM EVVSTPSQLK RYLSTAVEVD PERPVLVDKY
     LDQATELDVD ALCDSFGNVV IGGIMEHIEQ AGVHSGDSAC SLPTQTVPES ALATIREWTP
     KLARRLGVVG LLNMQYAVMP DGTPYIIEAN PRASRTVPFV SKAIGHPLAK YASLVMAGQS
     LEEIGFMQEP ITKHISVKEA VLPFDKFLGC DTLLGPEMRS TGEVMGIDFD FERAYCKAQI
     AAGQKLPKSG KVFISVKNSD KEAMVPVAKN LVDMGFEILS TGGTATTLES AGIKVTKVKK
     IHEGRPNIGD ILRDGDLKLM FVTSSGDAND LTDGRELRRT AVGLKVPICT TVAGIKATAG
     SLKILQEGNL QMQALQDFF
//

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