ID R5VC29_9BACT Unreviewed; 1071 AA.
AC R5VC29;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:CCZ81081.1};
GN ORFNames=BN709_00458 {ECO:0000313|EMBL:CCZ81081.1};
OS Odoribacter laneus CAG:561.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC Odoribacter.
OX NCBI_TaxID=1263089 {ECO:0000313|EMBL:CCZ81081.1, ECO:0000313|Proteomes:UP000017974};
RN [1] {ECO:0000313|EMBL:CCZ81081.1, ECO:0000313|Proteomes:UP000017974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:561 {ECO:0000313|Proteomes:UP000017974};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- 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:CCZ81081.1}.
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DR EMBL; CBAQ010000050; CCZ81081.1; -; Genomic_DNA.
DR RefSeq; WP_009137583.1; NZ_HF997792.1.
DR AlphaFoldDB; R5VC29; -.
DR Proteomes; UP000017974; 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 CDD; cd01423; MGS_CPS_I_III; 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 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; 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}; 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 Reference proteome {ECO:0000313|Proteomes:UP000017974};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 130..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 677..868
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 934..1071
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1071 AA; 119548 MW; 2983F885D779B826 CRC64;
MKEINKILLL GSGALKIGEA GEFDYSGSQA LKAIREEGKY SVLINPNIAT VQTSEGIADK
IYYLPVTPEF VEKVIEKERP DGILLSFGGQ TALNCGVALY KSGILEKYGV EVLGTPVQAI
IDTEDREIFS EKLHEIDVKT PRSIAANNME EAITAAKELG FPLIIRAAYT LGGLGSGFCS
DMEELKKLAG SAFSYSPQIL VEESLKGWKE IEYEVVRDQY DNCITVCNME NFDPLGIHTG
ESIVVAPSQT LSNSEYHKLR QIAIKIIRHI GIVGECNVQY TLDPNSEDYR VIEVNARLSR
SSALASKATG YPLAFVAAKL AMGYGLHEIK NSVTKVTTAC FEPALDYIVC KIPRWDLNKF
EGVSKLIGSS MKSVGEIMAI GRTFEEVIQK GLRMVGQGMH GFVGNNKDVK NIDEELTHPT
DVRIFAIAAA FDQGYSVEKI HEMTKIDNWF LERLENIHKL KNELSKYTTV RGVTPAMLKK
AKQMGFSDFQ IGRFTIKDTT LTAHQKMLKV REYRKELGIV PCIKQIDTLA GEYPAKTNYL
YATYNGSETD ITYERDGRSV IVLGSGAYRI GSSVEFDWCC VSAVNAIKKA GYRSVMINYN
PETVSTDYDT CDRLYFDELS FERVMDIVDL EEPKGVIVST GGQIPNNLAM RLYGQHVNIL
GTSALSIDRA EDRQKFSSMC DQLGIDQPRW RELTSIDDIY KFIDEVGFPL LIRPSYVLSG
AAMNVVSNKE ELLHFLELAA EVSKDHPVVV TEFVQQAKEV EIDAVAQEGI IKAYAISEHV
EFAGVHSGDA TIVFPAQKLY IETIRRIKKI ARAIAKELNI SGPFNMQFLA KDNDIKVIEC
NLRASRSFPF VSKVLKYNFV EMATRIMLGE HVEELHKSVF DLDYVGVKAS QFSFARLLKA
DPVLGVDMSS TGEVGCIGEN YYEAILKSML SVGHRIPEKN ILISSGPTRS KVELLESTRM
LIAKGYTIFA TAGTAKFFAD NGIEVSVLYW PDEAKEPNIM DYLKNKKIDM VINIPKNLTK
RELDNGYKIR RAAVDYNIPL LTNARLASAF IYAICKVDKE DIAIKSWDEY R
//
