ID A5KMF7_9FIRM Unreviewed; 1086 AA.
AC A5KMF7;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EDK24373.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EDK24373.1};
GN Name=carB {ECO:0000313|EMBL:EDK24373.1};
GN ORFNames=RUMTOR_01428 {ECO:0000313|EMBL:EDK24373.1};
OS [Ruminococcus] torques ATCC 27756.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=411460 {ECO:0000313|EMBL:EDK24373.1, ECO:0000313|Proteomes:UP000003577};
RN [1] {ECO:0000313|EMBL:EDK24373.1, ECO:0000313|Proteomes:UP000003577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27756 {ECO:0000313|EMBL:EDK24373.1,
RC ECO:0000313|Proteomes:UP000003577};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDK24373.1, ECO:0000313|Proteomes:UP000003577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27756 {ECO:0000313|EMBL:EDK24373.1,
RC ECO:0000313|Proteomes:UP000003577};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus torques (ATCC 27756).";
RL Submitted (APR-2007) 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 -!- 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:EDK24373.1}.
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DR EMBL; AAVP02000005; EDK24373.1; -; Genomic_DNA.
DR AlphaFoldDB; A5KMF7; -.
DR PaxDb; 411460-RUMTOR_01428; -.
DR HOGENOM; CLU_000513_1_0_9; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000003577; 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:0006520; P:amino acid metabolic process; IEA:UniProt.
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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:EDK24373.1};
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 144..338
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 683..874
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 944..1085
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1086 AA; 119392 MW; 5A82E683E00694CA CRC64;
MRTWDNTGGR KMAKRNDIHK VLIIGSGPII IGQACEFDYS GTQACKALRN LGYEIVLVNS
NPATIMTDPE IADVTYIEPL NVDRIEQIIK KERPDALLPN LGGQSGLNLC SELAQAGVLE
KYNVEVIGVQ VDAIERGEDR IEFKHTMDQL GIEMARSEVA YSVDEALAIA EKLGYPVVLR
PAYTMGGAGG GLVYNVDELK TVCARGLQAS LVGQVLVEES ILGWEELELE VVRDAEGNMI
TVCFIENIDP LGVHTGDSFC SAPMLTISEE VQQRLQEKSH KVVDSVKVIG GCNVQWAHDP
KTDRDIIIEI NPRTSRSSAL ASKATGFPIA LVSAMLATGM TLKDIPCGKY GTLDKYVPDG
DYVVIKFARW AFEKFKGVED KLGTQMRAVG EVMSIGKNFK EAFQKAIRSL ETGRYGLGHA
KDFDGKTKEE LLKSLRYATS ERYFVIYEAL RKGASVEEIH ELTKVKHYFL EQMKELVEEE
EALLAFKGGL PEDNALIAAK KDGFSDKYLS QILEVDEDEI RNKRISLGVE ETWEGVHVSG
TQDRAYYYST YNGTDKNPIS EEKPKIMILG GGPNRIGQGI EFDYCCVHAS LALKKLGFET
IIVNCNPETV STDYDTSDKL YFEPLTLEDV LSIYKKEKPV GVIAQFGGQT PLNLAADLER
NGVKILGTAP SVIDLAEDRD LFREMMDKLE IPMPESGMAV TVDDALEIAE KIGYPVMVRP
SYVLGGRGME VVYDAESMVG YMKAAVGVTP DRPILIDRFL GHATECEADA ISDGTHAFVP
AVMEHIELAG VHSGDSACII PSKNISEENV KTIKEYTRKI AEEMHVKGLM NMQYAIENGK
VYVLEANPRA SRTVPLVSKV CNIRMVPLAI DIVTSELTGR PSPVPALKEQ NIPYYGVKEA
VFPFNMFPEV DPLLGPEMRS TGEVLGLSKS FGEAFYKAQE ATQTKLPLEG TVLISVSNRD
KPEVVEVAAD FAKAGFKIIA SDHTCSLLKE NGIEAEKINK LQEGRPNMLD VITNGKVDMI
VNTPSGKESK NDDSYLRKAA IKKKVPYMTT MAAAKAAANG ILAVKKHGSK EVKSLQEIHG
EITDKE
//
