ID B8DQX8_DESVM Unreviewed; 1078 AA.
AC B8DQX8;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 93.
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 OrderedLocusNames=DvMF_2306 {ECO:0000313|EMBL:ACL09247.1};
OS Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=883 {ECO:0000313|EMBL:ACL09247.1};
RN [1] {ECO:0000313|EMBL:ACL09247.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Miyazaki F {ECO:0000313|EMBL:ACL09247.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA Richardson P.;
RT "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL Submitted (OCT-2008) 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|HAMAP-
CC 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}.
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DR EMBL; CP001197; ACL09247.1; -; Genomic_DNA.
DR AlphaFoldDB; B8DQX8; -.
DR STRING; 883.DvMF_2306; -.
DR KEGG; dvm:DvMF_2306; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_3_7; -.
DR OMA; IEPAGIH; -.
DR OrthoDB; 9804197at2; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
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}; Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
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};
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 683..874
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 941..1078
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 941..1078
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 833
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT BINDING 845
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT BINDING 845
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT BINDING 847
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
SQ SEQUENCE 1078 AA; 118045 MW; 9F36782E723DF23C CRC64;
MPKRTDLKRI MVIGSGPIVI GQACEFDYSG TQAVKALKEE GYEVVLVNSN PATIMTDPGL
ADRTYIEPIE PETVAAIIRK ERPDALLPTL GGQTGLNTAL ALAAMGVLEE CGVDLIGANK
QVIEKAESRE LFREAMANIG LKVPASGIAR TMEDVRRLGT EMPFPLIIRP AFTMGGTGGG
IAYNMEDLEE IAARGLAASI KHEVMIEQSV LGWKEFEMEV MRDKADNCVI ICSIENFDPM
GVHTGDSITV APAQTLTDVE YQMMRDASIA IMREIGVETG GSNVQFGINP QNGDMVVIEM
NPRVSRSSAL ASKATGFPIA KIAAKLAVGY TLDEIPNDIT RETMASFEPS IDYCVTKIPR
FTFEKFPGAK DELTTSMKSV GEAMSIGRTF KESLQKGLRS LEVGAPGLGS AFRCKGPERE
DIMRKLRTPN SRRIFYVRHA MLDGMTVEEI HEATAIDPWF LRQMKDLVDM EAELRDFALG
NAMTVDNAEL VALMRRAKEY GFSDRQLAEM WKRPESDVRT LRKQMGIAPT YYLVDTCASE
FEAYTPYYYS TYETGHEVAV EDRKKVIILG GGPNRIGQGI EFDYCCCHAS FALKEMGVQA
IMVNSNPETV STDYDTSDRL YFEPLTFEDV MNIIETEKPD GVVVQFGGQT PLNLAVPLMR
AGVPILGTSP DSIDRAEDRE RFQALLQKLG LRQPANATVM SLPEARSAAA RIGYPTVVRP
SYVLGGRAME IVYDEEQLAE YFANSVGEKP KHPILIDKFL ESAIEVDVDA LSDGTDVYVA
GIMEHIEEAG IHSGDSACVI PPHTLPEAIV NEIARQTVEL ARELRVVGLM NIQFAVKDGL
IYILEVNPRA SRTAPFVSKA TAVPLPRLAT QIMLGATLKE LDPWSMRRTG YFSVKESVFP
FNRFPGVDIL LGPEMRSTGE VMGIASSFEE AYLKGQLAGG QRLPQSGKIF ISVNDRDKLL
ITEVASMFAD LGFEVLATSG TAKLLREGGV PATSVHKVYE GRPNIVDFIK NGDIALVLNT
ASGKRTVQDS KSIRQATLMY GVPYSTTVSG AKAIAQAIRA SRCCGVNVKS LQEYYGTN
//