ID A0A1D1VWD0_RAMVA Unreviewed; 2257 AA.
AC A0A1D1VWD0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Aspartate carbamoyltransferase {ECO:0008006|Google:ProtNLM};
GN Name=RvY_15850 {ECO:0000313|EMBL:GAV05770.1};
GN Synonyms=RvY_15850.1 {ECO:0000313|EMBL:GAV05770.1};
GN ORFNames=RvY_15850-1 {ECO:0000313|EMBL:GAV05770.1};
OS Ramazzottius varieornatus (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Parachela;
OC Hypsibioidea; Ramazzottiidae; Ramazzottius.
OX NCBI_TaxID=947166 {ECO:0000313|EMBL:GAV05770.1, ECO:0000313|Proteomes:UP000186922};
RN [1] {ECO:0000313|EMBL:GAV05770.1, ECO:0000313|Proteomes:UP000186922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YOKOZUNA-1 {ECO:0000313|EMBL:GAV05770.1,
RC ECO:0000313|Proteomes:UP000186922};
RX PubMed=27649274; DOI=10.1038/ncomms12808;
RA Hashimoto T., Horikawa D.D., Saito Y., Kuwahara H., Kozuka-Hata H.,
RA Shin-I T., Minakuchi Y., Ohishi K., Motoyama A., Aizu T., Enomoto A.,
RA Kondo K., Tanaka S., Hara Y., Koshikawa S., Sagara H., Miura T.,
RA Yokobori S., Miyagawa K., Suzuki Y., Kubo T., Oyama M., Kohara Y.,
RA Fujiyama A., Arakawa K., Katayama T., Toyoda A., Kunieda T.;
RT "Extremotolerant tardigrade genome and improved radiotolerance of human
RT cultured cells by tardigrade-unique protein.";
RL Nat. Commun. 7:12808-12808(2016).
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 -!- 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:GAV05770.1}.
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DR EMBL; BDGG01000012; GAV05770.1; -; Genomic_DNA.
DR STRING; 947166.A0A1D1VWD0; -.
DR Proteomes; UP000186922; Unassembled WGS sequence.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
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; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR032466; Metal_Hydrolase.
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 NCBIfam; TIGR01368; CPSaseIIsmall; 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; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00101; ATCASE.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
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; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW 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:UP000186922};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 522..714
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1061..1252
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1318..1463
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1829..1884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1844..1884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 343
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2257 AA; 248209 MW; C71E624862B4784F CRC64;
MSAGALVLEE GSRFEGVVRG AIRNVSGEVV FQTGVVGYPE AVTDPSYHGQ ILVLTYPLIG
NYGVPGEEVE KNGLQKWLES GQVWPRAVVV GELSQQYSHW NAQRSFENWL LEHGVPILEG
VDTRSLTILL REFGTIAGKI VLEGTDPRSI PFVQCGLRNL VEEVSVKRMP PLINPRGDVK
ILVVDCGLKH NQIRCLIKRG AAVQVCPWNC PIEAEMDKYD GLFLTNGPGD PKLCGALVAN
LESYMKIKDT KPIFGICMGH QILARAAGLK TYRLKYGNRG HNQPCILNGT KRCFITSQNH
GYAVDVDKLP DRWEPLFTNA NDQTNEGLVH REKPIFSVQF HPEHRAGPQD LEALFDVFLD
SVRKYKNGAV EKPLPEVIRE KLQPLVPSCP VAAFRPHKVL VLGSGGLTIG QAGEFDYCGS
QALKALKDDK VKTVLMNPNI ATSQTTKGLA DKVYFLPITL EYVTQVIKAE RPDGILLNFG
GQVALNCGIK LSEADVLNKY NVAVLGTPVQ VIVWTEDRQE FAMKLSEIGY KVAPSAAVHS
VEEALEVAAK IGYPVLVRAA YSLGGLNSGF AETAHQLKEL AAKAFGVSSQ LMIDKSFKGW
KELEYEVVRD VFDNCITVCN MENIDPLGIH TGESMVVAPS QTLSNDEYNM LRTAAVDVIR
HLGVVGECNI QYALSPYSGE FFVIEVNARL SRSSALASKC TGYPLAYIAA KLAMGYSLAE
LRNPVTGTGT ACFEPSLDYC VVKIPRWDLR KFPGADNKIG SAMKSIGEGM AIGRSFEEAF
QKALRTTDET YTGFDPYICP LSEEILVNPT DKRVLVLATA LAEGYSVDRL HDLTKIDRWF
LAKMKNIIDF RQTIIRSCGE ESPQVDGNLL LKAKKLGFCD KQIAAYSRTT EPKVRELREL
HGIHPWVKQI DTVAGEWPAR ANYLYTTYHG AQHDVAFPGP ANAVAVLGSG VYRIGSSVEF
DCCAVGCLAE LRRLKRPTIM INCNPETVST DYDESDRLYF EELSFECVMD IYQLEEPAGI
ILAMGGQLPN NMAMALHRYG VKVLGSSPES IDSAENRFKF SRLLDGLKIG QPEWQELTDL
LSAKKFCERV GYPCLIRPSY VLSGAAMLVA YSAGDLEAYL GRDATVSKEY PVVISKFIEN
AKEIDVDAVA REGDVLCCAV SVHVEDAGVH SGDATLVTPP QNLDDATVQK IHLVARSIAE
GLDVNGPFNL QLLVKDGEVR VIELNLRVSR SFPFVSKTHG FDFVVAATRV ALGESVQIDN
FNIQNTTRIG VKASMFSFSR LTNADVSLGV EMRSTGEVAG FGENVHEALL KALLASGFRY
PRKGSTVFVG ISSGYHRKEL TESIQSLIEM GFRVMGNKTT AKYYITRGIE VLEIEQTVDI
GKSCSEHRFD LVISIPMRKG SVPRLSLDSQ QGHQLSRAAA DFDIPLITDF NMAKLFVESI
KKHPGHGPTL RIATDCVFSG SSVRLPGLID VGLMLEAESL ITTSSNAVSN GVTMTFVAAG
LHTCSTFAWC DFALVAEAST EKTVFGEKFM GQAFALELPL NGQEYRDMSV WRTQLKTWQK
GRPICVESSP AVVTKLLLIS SLFDHHVHFR NVCNKEVMFM IKEAKAAGLK ISCDVLVYCL
FFTDTVVHEC FAPDSPSKYH YSAEDQKSLW DNIVDVDCFS LSMNAKDQGL GGMGISLLLS
AVSDKRLTWD DITSRLYDGP KKIFGLTEQE NTYVEVDLSE EWLVPDLREQ HGKEDMRLRG
KIQRVVLRGV DVFMDGYVIA DTPTGQVIYS AVDKAPPLIF VSGGPDASRP RLFSMVRSRS
TMEKGAPGYE DEALSAFPMF DKHLEATRNR LDSQGRRRAS AVDLGRSQAS SERSSLQVPV
STASRSGRDS VLNTKHSPMS TSMRRPSLFL SPSFENLSSR RVSLVSVPTD APKKLPFLHV
VSAEDFCQVD VKNLMELAKH FQSSSKKNRP VGDLLCGKIL VTLVYGNDTL TAAGFDAAMK
RLGGSVIVVN TSTSSVQKGE SLSDTVKILT SYGDMIVVKQ GEVDAVKVAT WCGMKPFISA
GDPAGEDVVQ SLSDVFTIWD EFGTLKDLTV TFTGNLNRGS AIHSLIKLLA LSPISEIRYV
EISGLGIPCA VQEYVEDRQI RLTAYPSLSA ALPGTNVLYV GELYPSDFIE DFHYTSAVSA
STLSAPLLNS QKPEMRTGVT MLRILHLQPR SGATLMLPEL EKDHRVIYFG QAENGFYMRQ
ALLFTLLKGG SEDAKRSSVS LDIFRRRKSW VPVVPVK
//
