UniProt: F8KR15

Database: UniProt
Entry: F8KR15_HELBC

LinkDB:  F8KR15_HELBC 
Original site:  F8KR15_HELBC

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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   F8KR15_HELBC            Unreviewed;      1074 AA.
AC   F8KR15;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:CCB79183.1};
DE            EC=6.3.5.5 {ECO:0000313|EMBL:CCB79183.1};
GN   OrderedLocusNames=HBZC1_01970 {ECO:0000313|EMBL:CCB79183.1};
OS   Helicobacter bizzozeronii (strain CIII-1).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1002804 {ECO:0000313|EMBL:CCB79183.1, ECO:0000313|Proteomes:UP000008387};
RN   [1] {ECO:0000313|EMBL:CCB79183.1, ECO:0000313|Proteomes:UP000008387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIII-1 {ECO:0000313|EMBL:CCB79183.1,
RC   ECO:0000313|Proteomes:UP000008387};
RX   PubMed=21705603; DOI=10.1128/JB.05439-11;
RA   Schott T., Rossi M., Hanninen M.L.;
RT   "Genome sequence of Helicobacter bizzozeronii strain CIII-1, an isolate
RT   from human gastric mucosa.";
RL   J. Bacteriol. 193:4565-4566(2011).
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; FR871757; CCB79183.1; -; Genomic_DNA.
DR   RefSeq; WP_013889688.1; NC_015674.1.
DR   AlphaFoldDB; F8KR15; -.
DR   STRING; 1002804.HBZC1_01970; -.
DR   KEGG; hbi:HBZC1_01970; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_0_7; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000008387; 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; 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; 1.
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:CCB79183.1};
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:UP000008387};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          132..325
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          678..865
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          940..1074
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   1074 AA;  118496 MW;  C0B2A91CE096385D CRC64;
     MQNFKKILLI GSGPIVIGQA CEFDYSSSIA LKTLKGLGYE VVLLNSNPIT INTDKALAYK
     TYIEPINTAN VLKIVEQEGI EAILPTMGGQ TALNIMVELH QQGHFEGALK NVKLLGAKIE
     SILKAEDRRA FKECMLGIGL DLPKGGYAYS EEEALGVVKE VGFPCIIRSS FTLGGEGSAV
     AFNIEEFRDL AKFALEASPI SEILIEESLL GCKEFEMEVV RDCKDNCVIV CCIENVDPMG
     IHTGDSITIA PALTLTDKEY QRMRDASFAV LRAVGVDTGG ANVQFAIKDR RLLVIEMNPR
     VSRSSALASK ATLFPIAKVA TLLALGHTLE EIQNDITQST TCFEPTLDYI ITKIPHFDFE
     KFPQVDTTLG TSMKSIGEVM GIGGSFKESL MKALESDYLL KNLRAFLTSP LDLEFLKKEL
     RRPNPKRLLY AMHAFSDSLS VDEVHSLSFI DPYFLNEIKE IVQALLELKE ADKQALLSNK
     NTLFKLKSMG LSDVLIASFL GAHELEVRQA REALDLHPKM YQVDLSANEF KSPTPYLYST
     YAPPFPTPQK PPKSTRQKVI LIGSSANKIG VGMEFDYALT HASLALKKMG LSPIIINNNP
     ETISTDHDTS DTLYFEPITL EHVLEIVARE REHLLGVVVG FGGQTPLKIA KDLEALNIPL
     LGTAFKNIEI AEERDLCHKL LDHLNIAYPK GLCATSKVQA LECLENLELP LILRPSFVLG
     GAKMRILRTK EECLDYIENY SFETSLLMDS FLEDALELDV DAICDLKSVF VCSVLEHIEP
     AGIHSGDSTC FIPPSLSPQV LEEVYTQTQK IALGLQVLGL VNIQFAYKNN QLFVLEINPR
     CSRTIPFVSK ALGLDLAAMA IGVMVGQGLE DFKGLENKGG GLFLAKPLHY VFVKESVFPF
     NKLYGADLVL GPEMKSTGEV AGVGYTLAEA FYKSQLACNN PIKHSGHVFV SLKDSDKQRA
     MPLMRAFASL GFKLYATTGT HRALLAEGLE SVQVLKISEG RPNISDFMLN QQIDMAINTS
     DRISEDSKII RMQVLKNKIS YFTTLKAVEK VLLSLLEYSK FSHNPPVSLQ ELQG
//

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