ID A0A0W1SQE4_9EURY Unreviewed; 1076 AA.
AC A0A0W1SQE4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KTG28431.1};
DE Flags: Fragment;
GN ORFNames=AUR66_11755 {ECO:0000313|EMBL:KTG28431.1};
OS Haloferax profundi.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1544718 {ECO:0000313|EMBL:KTG28431.1, ECO:0000313|Proteomes:UP000053157};
RN [1] {ECO:0000313|EMBL:KTG28431.1, ECO:0000313|Proteomes:UP000053157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB29 {ECO:0000313|EMBL:KTG28431.1,
RC ECO:0000313|Proteomes:UP000053157};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloferax profundi sp. nov. isolated from the Discovery deep brine-
RT seawater interface in the Red Sea.";
RL Submitted (DEC-2015) 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:KTG28431.1}.
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DR EMBL; LOPV01000135; KTG28431.1; -; Genomic_DNA.
DR RefSeq; WP_058571717.1; NZ_LOPV01000135.1.
DR AlphaFoldDB; A0A0W1SQE4; -.
DR OrthoDB; 85487at2157; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000053157; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
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 HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR InterPro; IPR011761; ATP-grasp.
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; 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 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; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
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 142..354
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 705..901
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 1076
FT /evidence="ECO:0000313|EMBL:KTG28431.1"
SQ SEQUENCE 1076 AA; 116777 MW; 9B9ACE4D4D6864B2 CRC64;
MTDEDTTPGT PTGTEDRTIL LIGSGPIQIG QAAEFDYSGA QACRALREEG ARVVLVNSNP
ATIMTDPEMA DKVYIEPITT EAISEIIRKE RPDGVIAGLG GQTGLNVTAE LAEEGVLDEF
DVDIMGTPLD TIYATEDRDL FRQRMEKIGQ PVPRSTTISL EDGEKVQNIT EADLEERVDD
AVDEVGGLPV IARTTYTLGG SGSGVVHEMD ELVSRVRKGL RLSRNSEVLI TESISGWVEL
EYEVMRDADD SCIIICNMEN IDPMGIHTGE STVVTPSQVI PDEGHQEMRD AALEVIRELG
IQGGCNIQFA WHDDGTPGGE YRVVEVNPRV SRSSALASKA TGYPIARVTA KVALGKRLHE
ITNEITGETT AAFEPAIDYV VTKVPRWPKD KFTDVDFELS TAMKSTGEAM AIGRTFEESL
MKALRSSEYD PAADWDEVSD EELETEYLVK PTPDRPYAIF EAFERGYTVD DVVELTGIEE
WYVERFGRIV ESVEAASEGD FAAAASAGHT NASIATATGT SVGDVEQQVP GRTYKQVDTC
AGEFAAQTPY YYSARKPEFF RGPFEGESAG NELRVDRDME SVVVVGGGPI RIGQGVEFDY
CSVHAVQALR EMGIDAHVVN NNPETVSTDY DTSDGLFFEP ITAEEVADVI EAIDADGVML
QFGGQTSVNI GHPLETELKR RGVDCEILGT TIDAMDLAED RDRFNRLMDD LGILQPQGGS
ATSEAEALEL ANDLGYPVLV RPSYVLGGRA MDVVHSDEEL CEYIEEAVRV SPDKPILIDE
FLADGVELDV DAVSDGERVL IGGVMEHVEA AGVHSGDSAC MIPPRSLDDE TMARVREVTE
DIAKALGTVG LMNVQLAVKQ NDDGSNDVYV LEANPRSSRT VPFVSKATGV PIAKLAAKVM
AGNTLDELEA TEQIPEQVSV KEVVLPFDRL PGSDPRLGPE MKSTGEVMGT ATTFAKAYEK
AQIAANDAIP RDGTVFVDLH DSEFPAPDSE EGQELLDGFA EYYEVLTPGD VDDLLTLLRE
GDVDFVVSRD RETLIDCVEE EVGYFSTFAS AKAALEARAA TDEDIDVHPV SERPRI
//
