GenomeNet

Database: UniProt
Entry: A0A0W1QL04_9SPHN
LinkDB: A0A0W1QL04_9SPHN
Original site: A0A0W1QL04_9SPHN 
ID   A0A0W1QL04_9SPHN        Unreviewed;      1109 AA.
AC   A0A0W1QL04;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000256|HAMAP-Rule:MF_01210};
GN   ORFNames=ATB93_10160 {ECO:0000313|EMBL:KTF69217.1};
OS   Sphingomonas sp. WG.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1592629 {ECO:0000313|EMBL:KTF69217.1, ECO:0000313|Proteomes:UP000052965};
RN   [1] {ECO:0000313|EMBL:KTF69217.1, ECO:0000313|Proteomes:UP000052965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WG {ECO:0000313|EMBL:KTF69217.1,
RC   ECO:0000313|Proteomes:UP000052965};
RA   Li H., Feng Z., Sun Y., Jiao X., Zhou W., Zhu H.;
RT   "Draft Genome Sequence of Sphingomonas sp. WG, a welan gum producing
RT   strain.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001777, ECO:0000256|HAMAP-
CC         Rule:MF_01210};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01210};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01210};
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01210};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077,
CC       ECO:0000256|HAMAP-Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004812, ECO:0000256|HAMAP-Rule:MF_01210}.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by the
CC       large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01210}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|ARBA:ARBA00009799,
CC       ECO:0000256|HAMAP-Rule:MF_01210}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01210}.
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:KTF69217.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LNOS01000034; KTF69217.1; -; Genomic_DNA.
DR   RefSeq; WP_019367929.1; NZ_LNOS01000034.1.
DR   AlphaFoldDB; A0A0W1QL04; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000052965; 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-UniRule.
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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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_A; CPSase_L_chain_A; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01210};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01210};
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|HAMAP-
KW   Rule:MF_01210};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP-
KW   Rule:MF_01210}; Reference proteome {ECO:0000313|Proteomes:UP000052965};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01210}.
FT   DOMAIN          133..328
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          714..905
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          971..1109
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   REGION          1..402
FT                   /note="Carboxyphosphate synthetic domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   REGION          971..1109
FT                   /note="Allosteric domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         285
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         299
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         301
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         864
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         876
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         876
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         878
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1109 AA;  118908 MW;  E4B02CEAF05253D6 CRC64;
     MPKRTDISSI LVIGAGPIVI GQACEFDYSG TQAIKALKEE GYRIVLVNSN PATIMTDPEL
     ADATYIEPIT PAVVAKIIEK ERPDAVLPTM GGQTALNTAL ALFRDGTLEK FGVTMIGADA
     DAIDKAEDRL KFKDAMTKIG LESARSAIAH TEAEALTALD HVGLPAIIRP SFTMGGSGGG
     IAYNREEFIA IVRSGLDLSP TTEVLIEESL LGWKEYEMEV VRDRNDNAII VCSIENIDPM
     GTHTGDSITV APALTLTDKE YQIMRNASIA CLREIGVETG GSNVQFAVNP KDGRLIVIEM
     NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDEIDNDIT GATPASFEPT IDYVVTKIPR
     FAFEKFKGAE AVLGTAMKSV GEVMAIGRSI HESIQKALRG LETGLSGFND VDRLVGAPRD
     VIEAALTVRS PDRLLIAAQA MREGFSVKEV QRFTSYDPWF LERIAEILDA EKDVATNGLP
     QDAAGMRRLK AMGFSDKRLA YLALKSVNLR AGSEAMARSS GLIGEVANAI SGGVTEAEVR
     KLRHRLGVRP VFKRIDTCAA EFEAKTPYMY STYEAPSFGE PENEAEPSDR RKVVILGGGP
     NRIGQGIEFD YCCCHACFAL ADAGYETIMV NCNPETVSTD YDTSDRLYFE PLTAEDVLEI
     LEVEKSKGEL VGVIVQFGGQ TPLNLAKALE DAGIPILGTS PDAIDLAEDR ERFADLVAKL
     GLKQPANGIA RSRDEAVRVA ERIGYPVLMR PSYVLGGRAM EIVDSLQQLD DYIQTAVQVS
     GDSPVLIDQY LRDAIEVDVD AIADGTDVVV AGVLQHIEEA GVHSGDSACS IPPYSLPKEI
     IAEIERQTVA LARALKVKGL MNIQFAVKDG EVYLIEVNPR ASRTVPFVAK AIGAPIAKIA
     SRVMAGEKLA TLPKIDRDID YIAVKEAVFP WARFPGVDPV LSPEMKSTGE VMGIDRDFAT
     AFAKSQLGAG TVLPDGGTVF VSVKQGDKAV VLPGVKILAD LGFKIIATSG TAEFLAAEGI
     AVETVNKVAQ GRPHIVDRIQ DGDVALIFNT TEGWQSLKDS MSIRASALAQ KVPYFTTAPG
     SVAAARAIAA MRQNPFGVQP IQAYFASRG
//
DBGET integrated database retrieval system