ID A0A0A0BQA1_9CELL Unreviewed; 1127 AA.
AC A0A0A0BQA1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KGM09229.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:KGM09229.1};
DE Flags: Fragment;
GN Name=carB {ECO:0000313|EMBL:KGM09229.1};
GN ORFNames=N868_03090 {ECO:0000313|EMBL:KGM09229.1};
OS Cellulomonas carbonis T26.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=947969 {ECO:0000313|EMBL:KGM09229.1, ECO:0000313|Proteomes:UP000029839};
RN [1] {ECO:0000313|EMBL:KGM09229.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM09229.1,
RC ECO:0000313|Proteomes:UP000029839};
RA Chen F., Li Y., Wang G.;
RT "Genome sequencing of Cellulomonas carbonis T26.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM09229.1, ECO:0000313|Proteomes:UP000029839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T26 {ECO:0000313|EMBL:KGM09229.1,
RC ECO:0000313|Proteomes:UP000029839};
RX PubMed=26587181;
RA Zhuang W., Zhang S., Xia X., Wang G.;
RT "Draft genome sequence of Cellulomonas carbonis T26(T) and comparative
RT analysis of six Cellulomonas genomes.";
RL Stand. Genomic Sci. 10:104-104(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 -!- 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:KGM09229.1}.
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; AXCY01000112; KGM09229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A0BQA1; -.
DR OrthoDB; 9804197at2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000029839; 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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
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_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; 2.
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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KGM09229.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000029839};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 683..882
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 964..1109
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1107..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1127
FT /evidence="ECO:0000313|EMBL:KGM09229.1"
SQ SEQUENCE 1127 AA; 119266 MW; CB6C0FC88BEDED62 CRC64;
MPRRTDLTSV LVVGSGPIVI GQAAEFDYSG TQACRVLRSE GLRVILVNSN PATIMTDPEF
ADATYIEPIT PEVVEAIIAK ERPDAILPTL GGQTALNTAI ALDEAGVLER YGVEMIGVNT
ESIHLAEDRQ AFKQVVERAG AESARSVIAH SIDEVLAAAD ELGYPVVVRP SFTMGGLGSG
IAHDEEALRR IAGAGLHYSP TTEVLLEESI LGWKEYELEL MRDHADNVVV VCSIENVDPV
GVHTGDSVTV APALTLTDRE YQRLRDIGIA VIREVGVDTG GCNIQFAVHP ATGRVVVIEM
NPRVSRSSAL ASKATGFPIA KIAARLAVGY TLDEIPNDIT GSTPASFEPS LDYVVVKVPR
FAFEKFPSAD PLLTTTMKSV GEAMAMGRNF AEALGKAMRS IDKAGSVFHW DGDVPTGERL
AELMASIRIP TEGRLIDVQQ ALRSVGVDGG TSVQEVYEAT GIDPWFLDQV VLVNGIADEV
ATSPDLAPEL LRRAKRHGLS DQQIGRLRGI AESTVREVRQ ALGVRPVYKT VDTCAAEFAA
RTPYHYSSYD DETEVEPRER EAVIILGSGP NRIGQGIEFD YSCVHAALAL REHYETIMVN
CNPETVSTDY DTSDRLYFEP LTFEDVLEVY QAELAVGPVA GVIVQLGGQT PLALAERLEA
AGIPILGTPP AAIDAAEDRG VFGTVLTDAG LPAPAFGTAR SLAEATEVAR GIGYPVLVRP
SYVLGGRGME IVYSDGQLGE YVERALGAAA AANGGTGEIP PLLVDRFLDD AIELDVDALF
DGTELYLGGV MEHIEEAGIH SGDSACVLPP VTVSAAELDR IRVSTEAIAR GVGVRGLLNV
QFALVSDVLY VLEANPRASR TVPFVSKATG VPLAKAAALV MAGWSIAQLR ADGVLPADGD
GGDLGLDAPI AVKEAVLPFK RFRTARGSMV DTVLGPEMRS TGEVMGFDVD FPTAFAKSQA
AAFGGLPTSG RVFISVADRD KRSITFPVKR LSELGFEILA TQGTAAVLRR NGIASTVVRK
NSEGRGPAGE PTVVDLIEAG EVDMVVNTPS GQGAKADGYE IRTAAVTVDK PIVTTVQQLA
AAVQGIESLL AGPFSVRSLQ DHVLELRDRT RPAPRDGAAG SGGAGDG
//
