ID A0A101VP93_9PROT Unreviewed; 869 AA.
AC A0A101VP93;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KUO58392.1};
DE Flags: Fragment;
GN ORFNames=APF80_14395 {ECO:0000313|EMBL:KUO58392.1};
OS Alphaproteobacteria bacterium BRH_c36.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1734406 {ECO:0000313|EMBL:KUO58392.1, ECO:0000313|Proteomes:UP000053382};
RN [1] {ECO:0000313|EMBL:KUO58392.1, ECO:0000313|Proteomes:UP000053382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c36 {ECO:0000313|EMBL:KUO58392.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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}.
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:KUO58392.1}.
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DR EMBL; LOEV01000125; KUO58392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VP93; -.
DR STRING; 1734406.APF80_14395; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000053382; 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-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; -; 1.
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; 1.
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 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 32..104
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 465..665
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 731..869
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KUO58392.1"
SQ SEQUENCE 869 AA; 93872 MW; 92BDA24D7DD86F8D CRC64;
ADNCIIICSI ENIDPMGVHT GDSITVAPAL TLTDKEYQIM RNASIAVLRE IGVETGGSNV
QFAVNPADGR LVVIEMNPRV SRSSALASKA TGFPIAKVAA KLAVGYTLDE LENDITGGAT
PASFEPTIDY VVTKIPRFAF EKFFGADTTL TTSMKSVGEA MAIGRNFAES LQKALRSLEI
GLNGLDDIEL DGLGLGDDKN VIRAEVSKPT PERLLKVAQA LRLGVDVEQV HAYSRIDPWF
LERIREIVVM EKRVIDHGLP TTARSMRALK SMGFSDTRLA KLAGLDAAEV TARRKGLGVR
PVYKRIDTCA AEFASPTAYM YSTYEAPLDG EPVCEAEPSD REKIIILGGG PNRIGQGIEF
DYCCCHACFA LTDAGYETVM INCNPETVST DYDTSDRLYF EPLTAEDVLA VIEAEQARGS
VKGVIVQFGG QTPLKLASAL EAAGVPILGT SPDAIDLAEE RGRFQELINE LGLLQPPAGI
ARSPQEARAV ADATGYPVVI RPSHVLGGRA MEIVHDGAEI DRYIKRLSDI LDRPNELIVS
EKRPLLIDSY LTDAVEVDVD CLSDGKDTFV AGVMEHIEEA GIHSGDSACS LPPHSLGPEI
IAEMERQAKE LAKALNVVGL MNVQFAIKDG HVYILEVNPR ASRTVPFVAK VIGQPIASIA
AQVMAGRPLA DFNLKPPVFN HIAVKEAVFP FARFSGVDPI LGPEMRSTGE VMGIDRDFAM
AFGKSQLGAG QTLPMTGAVF VSVKDEDKPR IVEPLRELVE IGFKVMATRG TKRFLESHGV
ACEAVNKVLE GRPHIVDAMK NGQVQLVFNT TEGAKALADS KDIRRTALLH HIPYYTTLAG
ARAVIRAIRA LKSDSLEVAP LQSYTIRIT
//
