ID B0MQ38_9FIRM Unreviewed; 1072 AA.
AC B0MQ38;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EDS00173.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EDS00173.1};
GN Name=carB {ECO:0000313|EMBL:EDS00173.1};
GN ORFNames=EUBSIR_01847 {ECO:0000313|EMBL:EDS00173.1};
OS [Eubacterium] siraeum DSM 15702.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Oscillospiraceae incertae sedis.
OX NCBI_TaxID=428128 {ECO:0000313|EMBL:EDS00173.1, ECO:0000313|Proteomes:UP000005326};
RN [1] {ECO:0000313|EMBL:EDS00173.1, ECO:0000313|Proteomes:UP000005326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15702 {ECO:0000313|EMBL:EDS00173.1,
RC ECO:0000313|Proteomes:UP000005326};
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 (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS00173.1, ECO:0000313|Proteomes:UP000005326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15702 {ECO:0000313|EMBL:EDS00173.1,
RC ECO:0000313|Proteomes:UP000005326};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Eubacterium siraeum (DSM 15702).";
RL Submitted (NOV-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:EDS00173.1}.
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DR EMBL; ABCA03000050; EDS00173.1; -; Genomic_DNA.
DR AlphaFoldDB; B0MQ38; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000005326; 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; 2.
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:EDS00173.1};
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 133..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 672..863
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 933..1072
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1072 AA; 118199 MW; D2108F80BB9E93B1 CRC64;
MPKRQDINKI MIIGSGPIII GQACEFDYSG TQACKALKKL GYEIVLVNSN PATIMTDPDV
ADITYIEPLN LDRLTQIIEQ ERPDALLPNL GGQSGLNLCS ELDKAGVLKK FNVQVIGVQV
DAIERGEDRI EFKNAMKDLG IGMPRSEVAY TIDEAVKIAE ELKYPVVLRP AYTMGGAGGG
MVYNVDELKV VCERGLQASL VGQVLVEECI FGWEELELEV VRDADNNKIT VCFIENIDPI
GVHTGDSFCS APMLTIPEDV QKELQEMSYR IIESIEVIGG CNCQFARNPE TGRIVVIEIN
PRTSRSSALA SKATGFPIAF VSALLACGLT LKDIPCGKYG TLDKYYPDGD YIVIKFARWA
FEKFKGAEDK LGTQMRAVGE VMSIGKTYKE AFQKAIRSLE KDRYGLGFAK NFHDMTKEEL
LAQLRYPTSE RQFVIYEALR KGATIEEIHA LTKIKDWFLQ QMKELVDEEE ALLKIKGSVP
EKAVLKQAKL DGFSDRYLSS LLEVTEEEIR NARIGFGIKE AWEGVHVSGT DNAAYYYSTY
HLDEDKSPVS DKPKIMILGG GPNRIGQGIE FDYCCVHAAL ALKKLGFESI IVNCNPETVS
TDYDTSDKLY FEPLTLEDVL SIHDKEKPLG VIAQFGGQTP LNLASDLKKY GVNILGTTPE
TIDLAEDRDH FRAMMDKLGI PMPESGMAVN VDEALKIANR IGYPVMVRPS YVLGGRGMEI
VHDDEMMKVY MSAAVGVTPD RPILIDRFLH HATECEADAI SDGKNCFVPA VMEHIELAGV
HSGDSACILP SMNLTEKQVA TIKDYTKKIA VEMNVCGLMN MQYAIEDDTV YVLEANPRAS
RTVPLVSKVC DINMVQLATQ IITSSLTGKP SPVPELHDKV INHYGVKEAV FPFNMFQEVD
PVLGPEMRST GEVLGIAPTF GEAYYKAQEA TQVKLPLGGT VLLSVCDRDK PELLEIAKSF
SELGFRILAT GKSYDMIKDA GITAERINKM YEGRPNITDA IANGDIQLII NTPAGKTSAN
DDSYIRKSAI RHKVPYITTM AAAKASIEGI KSLKANKHFG VKSIQAHHAD IK
//
