ID F9D6L4_PREDD Unreviewed; 1074 AA.
AC F9D6L4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EGQ11931.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EGQ11931.1};
GN Name=carB {ECO:0000313|EMBL:EGQ11931.1};
GN OrderedLocusNames=Prede_2329 {ECO:0000313|EMBL:AGB29595.1};
GN ORFNames=HMPREF9136_2492 {ECO:0000313|EMBL:EGQ11931.1};
OS Prevotella dentalis (strain ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043
OS / ES 2772) (Mitsuokella dentalis).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=908937 {ECO:0000313|EMBL:EGQ11931.1, ECO:0000313|Proteomes:UP000007820};
RN [1] {ECO:0000313|EMBL:EGQ11931.1, ECO:0000313|Proteomes:UP000007820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3688 {ECO:0000313|EMBL:EGQ11931.1,
RC ECO:0000313|Proteomes:UP000007820};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000010862}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043 / ES 2772
RC {ECO:0000313|Proteomes:UP000010862};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome 2 of Prevotella dentalis DSM 3688.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AGB29595.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 3688 {ECO:0000313|EMBL:AGB29595.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Chertkov O.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Complete sequence of chromosome 2 of Prevotella dentalis DSM 3688.";
RL Submitted (FEB-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}.
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DR EMBL; CP003369; AGB29595.1; -; Genomic_DNA.
DR EMBL; AFPW01000047; EGQ11931.1; -; Genomic_DNA.
DR RefSeq; WP_005847574.1; NZ_GL982490.1.
DR AlphaFoldDB; F9D6L4; -.
DR STRING; 908937.Prede_2329; -.
DR KEGG; pdt:Prede_2329; -.
DR PATRIC; fig|908937.9.peg.2462; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_3_10; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000007820; Unassembled WGS sequence.
DR Proteomes; UP000010862; Chromosome 2.
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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EGQ11931.1};
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:UP000010862};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 132..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 680..871
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 933..1074
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1074 AA; 119923 MW; D5EDF50E552B306D CRC64;
MKDTNIKKVL LLGSGALKIG EAGEFDYSGS QALKALREEG VRTVLINPNI ATVQTSEGVA
DQIYFLPVQP YFVERVIEKE RPDGILLSFG GQTALNCGVE LYESGVLEKY GVKVLGTPVQ
AIMDTEDREL FVRKLDEIDV KTIKSEACET MEQSLQAANH LGYPVIVRAA YALGGLGSGF
ANNDDELRTL CEKAFSFSPQ VLVEKSLKGW KEIEYEVVRD CYDNCITVCN MENFDPLGIH
TGESIVIAPS QTLTNAEYHK LRALSIKIVR HIGIVGECNV QYAFDPASED YRVIEVNARL
SRSSALASKA TGYPLAFVAA KLGMGYGLFE LKNSVTKTTS AFFEPALDYV VCKIPRWDLS
KFHGVDRELG SSMKSVGEVM AIGRNFEEAI QKGLRMIGQG MHGFVENKEL EIPNLDEALQ
EPTDKRVFVI SKAMHRGYTI DQIHELTKID RWFLHKLKHI IDIDERLKRC NVNTLDRTLL
REAKVYGFTD FQVARAVGLE RELGNMHKAM LLIRRLRKGY GIVPVVKQID TLAAEYPAQT
NYLYVTYAGV ASDVAFPSDR HSVVVLGSGA YRIGSSVEFD WCGVQALQTI RRQGYRSIMI
NYNPETVSTD YDMCDRLYFD ELTFERVMDI IELENPHGVI VSTGGQIPNN LAMHLDEQHV
PILGTSARDI DNAEDRAKFS SMLTRNNINQ PEWSALTSMD DIDRFVERVG FPVLVRPSYV
LSGAAMNVCS NREELERFLR LAANVSEDHP VVVSKFIEHA KEIEMDAVAR DGEILAYAIS
EHIEFAGVHS GDATIEFPPQ KLYVETVRRI KRVSRQIARE LHISGPFNIQ YMARENDILV
IECNLRASRS FPFVSKVLKL NLIDLATKVM LGVPVERPSK NLFDLEYVGI KASQFSFNRL
QKADPVLGVD MSSTGEVGCL GDDTNQALLK SMLSVGHRIP RHSVLLSTGG AKQKVEMLDA
AKMLIDHGYE LYATGGTSKY LKDNGIDNTL VYWPSDEGKE PQALTLLHEK KIDMVVNIPK
DLTTHELTNG YKIRRAAIDL NVPLITNTRL ASAFITAFCT LGPADIDIKA WGEY
//
