ID B2KDJ0_ELUMP Unreviewed; 1102 AA.
AC B2KDJ0;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:ACC98586.1};
DE EC=6.3.4.16 {ECO:0000313|EMBL:ACC98586.1};
GN OrderedLocusNames=Emin_1033 {ECO:0000313|EMBL:ACC98586.1};
OS Elusimicrobium minutum (strain Pei191).
OC Bacteria; Elusimicrobiota; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=445932 {ECO:0000313|EMBL:ACC98586.1, ECO:0000313|Proteomes:UP000001029};
RN [1] {ECO:0000313|EMBL:ACC98586.1, ECO:0000313|Proteomes:UP000001029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pei191 {ECO:0000313|EMBL:ACC98586.1,
RC ECO:0000313|Proteomes:UP000001029};
RX PubMed=19270133; DOI=10.1128/AEM.02698-08;
RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA Lapidus A., Hugenholtz P., Brune A.;
RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL Appl. Environ. Microbiol. 75:2841-2849(2009).
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}.
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DR EMBL; CP001055; ACC98586.1; -; Genomic_DNA.
DR RefSeq; WP_012415201.1; NC_010644.1.
DR AlphaFoldDB; B2KDJ0; -.
DR STRING; 445932.Emin_1033; -.
DR KEGG; emi:Emin_1033; -.
DR HOGENOM; CLU_000513_1_3_0; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000001029; 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: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; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ACC98586.1};
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:UP000001029};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 140..332
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 713..904
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 968..1102
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1102 AA; 122539 MW; BD0500158FA32538 CRC64;
MPILNFLKPK NGKKQKVLLL GSGALSIGQA GEFDYSGSQA IKALEEEGLE VIVLNPNIAS
VQTNPAPNKK IYLYPVTPFW IEKIIKKERP VALIAGFGGQ TSLNCAIELH NNGVLKKYGV
KVLGTPVSSL EMSEDRDLFS KRMHEIGVPT PPSKAVETVE EALKTALEIG YPVITRSAYA
LGGLGSGLAE NPEQLEKLAS SALTSSPQIL IEKSLHGWKE IEYEVMRDAC GNSITICNME
NFDPMGIHTG DSIVIAPCQT LNNRENNMLR DAALNIVKSI GVVGECNVQF ALSPFTLEYY
VIEINARLSR SSALASKATG YPIAFVAAKV VSGFDLLELK NPVTGTTSAF YEPSLDYVSL
KVPRWDLKKF TGVSKELGTQ MKSVGEVMSI GRNFCEVVQK ALRMVQEDEE GLMKEVFAGT
SDKELLKEAA HPTNLRIFAI YELFKRGFSV DKVKNVTKIE PWFLSHLFYL AKLENEVATF
FKGVKAPKKL TADFIKKQFT NIDTEYLRRL KSRGFSDYQL TKLLLSVISP KEKFTNKEIN
SLSLGLRELR KKMNIVPVVK QIDTTSAEYY TTSNYLYLTY DGTHNDITLK KKNKSIITLG
SGSYRIGSSL EFDWCSVMTS KYFKQQKDDS IIINCNPETV STDFNSSDRL YFEELSFERV
MDIIDFESPK GVVACMGGQN PNNLTPYLSR VGVNILGHSF ETVEKAENRT KFSAILDSLN
IDQPKWTSAA SRKEVNDFVK EVGFPVLIRP SFVLSGTLMN VANDQKSLDY YLSLTKDISA
DYPVVLSQFI LDAKELECDG VAKNGEVLLS FISEHVENAG VHSGDATLVF PAEKIYTKTA
NSIRDIVRKI AKGLNLNGPF NIQFIAKDND VKVIECNARA SRSFPFITKV SGQNLAEFSC
KVMNNEKVDK VFMDESEIPY TGVKASMFSF QRLDGADPIL GVEMASTGEV GCIGANFNEA
MLLAMESTHI KMPKKGILLS TGREKDKIKF MEVIDNVYKF GLPVYATLGT ANYLKEHGYD
AIPVMYHHDP KPVDVIKQRK VDFVVNVHKS LELDELEHNS AIRKTAVKSN CSLLTNLEKA
IAYFKAFDSY KALSEKDDLI HL
//
