ID A0A0F5JFU5_9BACT Unreviewed; 1072 AA.
AC A0A0F5JFU5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:KKB56696.1};
GN ORFNames=HMPREF1536_02332 {ECO:0000313|EMBL:KKB56696.1};
OS Parabacteroides gordonii MS-1 = DSM 23371.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=1203610 {ECO:0000313|EMBL:KKB56696.1, ECO:0000313|Proteomes:UP000033035};
RN [1] {ECO:0000313|EMBL:KKB56696.1, ECO:0000313|Proteomes:UP000033035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS-1 {ECO:0000313|EMBL:KKB56696.1,
RC ECO:0000313|Proteomes:UP000033035};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Martens E., Sakamoto M.,
RA Benno Y., Suzuki N., Matsunaga N., Koshihara K., Seki M., Komiya H.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Parabacteroides gordonii DSM 23371.";
RL Submitted (APR-2013) 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:KKB56696.1}.
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; AQHW01000014; KKB56696.1; -; Genomic_DNA.
DR RefSeq; WP_028728090.1; NZ_KQ033919.1.
DR AlphaFoldDB; A0A0F5JFU5; -.
DR STRING; 1203610.HMPREF1536_02332; -.
DR PATRIC; fig|1203610.3.peg.2394; -.
DR HOGENOM; CLU_000513_1_3_10; -.
DR Proteomes; UP000033035; 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; 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; 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:UP000033035};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 132..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 678..869
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 935..1072
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1072 AA; 118900 MW; 143B6E5E261BBD31 CRC64;
MSKIGIKKVI VLGSGALKIG QAGEFDYSGS QALKALKEEG ISTVLLNPNI ATIQTSEGVA
DKVYFLPITP YFVEEVIKKE QPDGILLAFG GQTALNCGTQ LYTSGTLAKY GVKVLGTSVE
AIMYTEDRDL FVKKLNEIDV KTPVSQAVET MDDAVKAAYK IGFPVMIRSA YALGGMGSGI
CKDEAELRTL AESAFAYSSQ ILVEESLKGW KEIEFEVIRD KNDHCFTVVS MENVDPLGVH
TGESIVVAPT CSLTDKELDL LKELSTKTIR HLGIVGECNI QYAFNSDTCD YRVIEVNARL
SRSSALASKA SGYPLAFVAA KLALGYSLDE IGEMGTPNSA YKAPEVDYMI VKIPRWDLTK
FVGVSRLIGS SMKSVGEIMS IGKSFEEIMQ KGLRMIGQGM HGFVGNNDLE FDNLDDALAN
PTDLRIFAVA KALEEGYTVE RIHELSKITP WFLNGLKNIV DYTKVLSQYN KIEDLPEEVM
KEAKRLGFSD FQIARYVENP EGNMEKENIR VRNLRKKMGI LPSVKRINTI ASEHPELTNY
LYMTYDGSEH DIPYYKNDKS VVILGSGAYR IGSSVEFDWC SVNAAQTARK LGYKSIMINY
NPETVSTDYD MCDRLYFDEL SFERVLDVMD LEMPKGVIVS VGGQIPNNLA MKLYRQNVPV
LGTSPLSIDR AENRHKFSAM LDTLGIDQPR WAELTSMEEI DGFIEKVGFP ILIRPSYVLS
GAAMNVCHNK EQMIEFLDLA AKVSKEYPVV VSEFLQGAKE VEFDAVAMNG EVVEYAISEH
IEFAGVHSGD ATLVFPAQKI YFETARRIKK VSKMIAKELN ISGPFNIQFL AKNNDVKVIE
CNLRASRSFP FVSKVLKRNF IETATRIMLD APYTKPDKSA FDIDWIGIKA SQFSFARLHK
ADPVLGVDMS STGEVGCIGD DFNEALLSAM IAVGNTIPKK NVLVSSGAAK SKVDLLEPCR
LLNEKGYQIY GTAGTAKFLN ENGIAATAVC WPDEQGDLNI MDMFSNHVFE LVVNIPKDHS
KRELTNGYKI RRAAIDHNIP LITNARLASA FIEAFCTMDV KDIQIKDWQD YK
//
