ID A0A101GJ76_9BACT Unreviewed; 1061 AA.
AC A0A101GJ76;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:KUK59444.1};
GN ORFNames=XD80_0086 {ECO:0000313|EMBL:KUK59444.1};
OS Synergistales bacterium 53_16.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635273 {ECO:0000313|EMBL:KUK59444.1, ECO:0000313|Proteomes:UP000053116};
RN [1] {ECO:0000313|Proteomes:UP000053116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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 -!- 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:KUK59444.1}.
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; LGGB01000002; KUK59444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101GJ76; -.
DR PATRIC; fig|1635273.3.peg.1687; -.
DR Proteomes; UP000053116; 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:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
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 138..332
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 679..869
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 938..1061
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1061 AA; 113889 MW; E1DA92E249E3871A CRC64;
MVRNVMMEPG THKQILVIGS GPIRIGQAAE FDYSGCQACR ALKEEGCRVI LLNSNPATIQ
TDVSLADVIY IRPLLADVVE DILKTHKPDA VLATLGGQVA LNLAVELEEK GIWERYGVKV
LGTSTDSIKK SEGREAFRKV MESIGEPVIE SAYVSCVEAA TVFAGEAGFP LVIRPDFTLG
GTGGGVARGP EALSRIVEEG LRASPVHRVL VERYLEGWHE IELEVMRDGA GNVLCVCGME
NIDPMGIHTG DSIVAAPTLT LTDSLWQRFK ASAFRIVDAL DVRGACNVQY ALSPAAERFA
VIEVNPRASR SSALASKATG YPIARIAAKI ALGKNLTELP NPVTGKGNAL SEPTPDYVVV
KFPRWPFEKF PQADASVGTR MKSTGEVMSI GTSFIEALMK AIRSLDGPFG ISDPLVETTD
SEALYAELKT PTHRRLWAML ELLRRGEREK PISKASGIHE FFVKELAKIS RLRTDLERKG
PQEHLLKEAA IYNFPEDETA AFCGITREEL RESRGWKEHP RVYRMIGRPS GEVASGSGYW
YATRGGFEGD QLPDGQDRRT AIAVLGSGPI RIGQGVEFDY CCVKAVEALK KRNKRAIIIN
NNPETVSTDH DVSDALYFEP LSTEDVLPII KREKVEGMFA CFGGQTSLKL GLDLDEAGIP
LLGTPCAGIK TAEDREKFSS LLNSLGIPQP KGAAVASVQA GLKCAAEVGY PVMIRPSFVI
GGLAMQAVST PDDLEEVLKM ALEIKAGQTV LIDRFLPGRE FEVDALYDGK DVLIPGVFEH
LDPPGVHSGD SIAVFPDVSL SVGLKEKILE TTVKIAEALQ VRGMMNIQFV QDGDDLYVIE
ANPRASRTIP IATKLTGIPL VEIAVDIALG KGIATLGWPT GLQKRMGPMG VKVPVFSTEK
LPGVDSRLGP AMQSTGESLG VADNVSEALW EALRGAGWVL PEKGKMLLSV SDAAKGNISG
IASAFCTLGW SIDATKGTAE VLEKWGIPCG VAEKGEGLQN SIKKGNWDLV INIPSASTLS
VRDGFAIRRS AIEAGVPCLG TLQSASAIGV ALSLKKGGDR C
//
