ID W0DEX8_9AQUI Unreviewed; 557 AA.
AC W0DEX8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:AHE95465.1};
GN ORFNames=THERU_00970 {ECO:0000313|EMBL:AHE95465.1};
OS Thermocrinis ruber.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX NCBI_TaxID=75906 {ECO:0000313|Proteomes:UP000018914};
RN [1] {ECO:0000313|EMBL:AHE95465.1, ECO:0000313|Proteomes:UP000018914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23557 {ECO:0000313|EMBL:AHE95465.1,
RC ECO:0000313|Proteomes:UP000018914};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-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}.
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DR EMBL; CP007028; AHE95465.1; -; Genomic_DNA.
DR RefSeq; WP_025305413.1; NZ_CP007028.1.
DR AlphaFoldDB; W0DEX8; -.
DR STRING; 75906.THERU_00970; -.
DR KEGG; trd:THERU_00970; -.
DR PATRIC; fig|75906.3.peg.191; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_1_0; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000018914; Chromosome.
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 Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation 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; 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; 1.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 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}.
FT DOMAIN 133..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 557 AA; 62678 MW; AD4B6741DD3B7FCA CRC64;
MPKDTSIKSI LIIGSGPIVI GQAAEFDYSG TQACKALKEE GYRVILVNSN PATIMTDPNM
ADRTYIEPLT LDILEAIIKK ERPDALLPTL GGQTALNLAV NLYEEGILDR YGVRLIGANY
QAIKKGEDRK LFAQSMRKIG LKVPENAVVS SVEEALKAVK DIGFPVILRP AFTLGGTGGS
IAYNIEEFKE KVEIALKTSP IHQVLLDKSL IGWKEYEFEV VRDKKDNVII VCSIENFDPM
GVHTGDSITV APAQTLTDKE YQILRDACIE IMREIGVDTG GSNIQFAVNP ENGDFYVIEM
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELKNEIT KHTPASFEPS IDYVVVKIPR
FDFAKFPETD RTLTTMMKSV GEVMAIGRTF KEALLKAIRS LEMDRYGLYL PQVQKLSDEE
LRKMIRTPNP DRLWHLAEAF RRGWSVEELY ELSHIDRWFL YNLKQVVDFE KRLVEEALDG
ELLRQAKELG YSDIEIARLK GTTEDQIRQL RETYGIVPAF KGVDTCAGEF FAYTPYYYST
YERPYYHLQE GVILDED
//
