ID A0A0G0XFX5_9BACT Unreviewed; 1112 AA.
AC A0A0G0XFX5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=CRE-PYR-1 protein {ECO:0000313|EMBL:KKS23769.1};
GN ORFNames=UU81_C0019G0007 {ECO:0000313|EMBL:KKS23769.1};
OS Microgenomates group bacterium GW2011_GWC1_41_8.
OC Bacteria.
OX NCBI_TaxID=1618519 {ECO:0000313|EMBL:KKS23769.1, ECO:0000313|Proteomes:UP000034304};
RN [1] {ECO:0000313|EMBL:KKS23769.1, ECO:0000313|Proteomes:UP000034304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS23769.1}.
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DR EMBL; LCCB01000019; KKS23769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0XFX5; -.
DR PATRIC; fig|1618519.3.peg.527; -.
DR Proteomes; UP000034304; 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 Gene3D; 3.40.50.20; -; 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; 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 PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 3.
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; 1.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 128..352
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 707..898
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 960..1112
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 281..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1112 AA; 125129 MW; E7B499394161B45C CRC64;
MIKKVLILGS GALKIGQAGE FDYSGSQAIK ALKEEGITSV LINPNIATVQ TSDYMADEVY
FLPVDPYFVE KVIEKEKPDG IFLSFGGQTA LNCGVELHKS GVLKKHNVSI LGSPIESIIL
TEDREKFAKH LRKIHRSIPH SISATTMKKA QHGAREIGYP VMIRAAYVLG GQSSGIVQNE
QELTKLCEEA FSFAPQVLVE QYLHHYKEIE YEVVRDKNDN CITVCNMENF DPLGIHTGES
IVIAPSQTLN NYEYHTLRQA SIDIIRSLGI VGECNIQYAV SPNPSSSSSF PRRRESINNK
QEIPDHASRV RNDNNNLEYY VIEVNARLSR SSALASKATG YPLAYVAAKL ALGKTLNEIP
NQVTKVTQSF FEPALDYCVV KIPRWDIDKF RKAHEKIGSS MKSVGEVMGI GRSFSEALQK
AVRMLEIGVD GITDHSYLFK KSNGNFTQQQ IIDEHILCPT PRRLFAVTYL LQHNYSLEKL
YQQTGIDPWF LNRIHEAVQL EKKINAKKLS EIDSKQLRKL KQYGFSDHRI AVITGTLEDH
VRNRRKKDHI LPSVFQIDTL AAEFPAQTNY LYLTYHGNHH DIEPRGDEGI MVLGSGPYRI
GSSVEFDWSC VSAARRLVRY NKKSIIVNCN PETVSTDYDV SDRLYFEELS LERVLDIYDF
EKSHGVIISV GGQTPNNLAV PLKENKVRIL GTDPDNIDRA EDRNTFSKTL DKLNIKQPEW
IQATTIEQAE LFAQNVGYPI LVRPSYVLSG SAMSVCSNDA ELKNYLERAV SINKSRPVTV
SKFYEGAKEI EIDAVAWRGT LDVYAISEHV EYAGVHSGDA TIVFPAQRVY EPTKQIILDY
TRKLARTYQI TGPFNIQFLA IRNDVSIIEM NLRASRTFPL LSKATGINFA EKVVDAFFDD
GRVEKEVFPP YTVVKVPQFS FARLTGADPV LDVEMNSTGE VGCFGDDVDE AFLKSMLSVG
YAFPHKNILV SIGDWYKEQF ASKLVQLHAM GYTLYATEGT ADFMKQKLGI PAISVKKGYE
GGKQNVLSLI EQKKVELVIN IRDRWHKSAD AKTYRKETTD GYLIRRSASD HNISSLTDIK
KSSLFVSALS EKKLADLKIK SWKEYLSLNI LK
//
