ID A0A1Q9EI78_SYMMI Unreviewed; 2208 AA.
AC A0A1Q9EI78;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Protein pyrABCN {ECO:0000313|EMBL:OLQ07078.1};
GN Name=pyrABCN {ECO:0000313|EMBL:OLQ07078.1};
GN ORFNames=AK812_SmicGene9554 {ECO:0000313|EMBL:OLQ07078.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ07078.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLQ07078.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ07078.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) 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 -!- 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:OLQ07078.1}.
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DR EMBL; LSRX01000147; OLQ07078.1; -; Genomic_DNA.
DR OMA; WSPFNGK; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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; 3.30.1490.20; 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; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
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 PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 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; 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; 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}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000186817};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2208
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012367353"
FT TRANSMEM 2120..2141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2153..2171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2177..2195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 942..1134
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1570..1761
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1827..1979
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 692
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 776
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 778
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2208 AA; 244162 MW; D4956737E2D58051 CRC64;
MSRAVVGIHV ALYCLAAAHG SAEGTIRGAS HARFLDVQYF NRTDVDSLLA RQMTHDPKTT
PRLRHLRVDL EPIFRTLAKT PNGGLSHQAA KYALFRFFLH ERSWLVKGLE PEGIWQTQPE
RLRKVWESWV PSYLQQRFEE AKQSEGASLD DLVEMIAVIE DLVQQESRKQ MAKVFESLDL
PLNGPLSRAD ADMAVDMYLL VVLTAQNLTL AEPAKNRKRV SRLHRRVEHG EALRWLRHLE
DRILVEQGKV YDFSSISKVA EAFGLEFPSF NDKECSDLKA RLVSMEGGSR KPGRIPLTDF
YGSIAYRHWN FSESPDYLRD LGVLDESDPH RPHVILANYI TSYNNCMRTD GLYAICCRSV
CGDMMSAIEQ QPFWLKNFWL SEAPCSLRCM CDWPESPEKM GWDFVGFEGV EAMDAKPTGQ
PMDFLRWLNA RRKCNLELVD GTVLKGYSFG APVSVSGEVV FNTGMVAYPE SLTDPSYAGQ
ILVITYPLVG NYGVPSDDKD EFGLPKWFES HKIHLKGVVI SDYSYEPSHY SCVRTLGQWL
ESQGVPGIYA VDTRLVTKQI REIGSMLGKL IVQGSTPSSH LPVDDPNKRN LVAEVSRTQK
EVFAPSQPNP RLNRDVHVLA VDCGMKNNII RCLVKLGLRV TVVPWDYDFT QDSFDGLFLS
NGPGDPTQCA KTVEHVKTIM RERPKTPIFG ICLGNQILAL AAGASTYKMK FGNRGMNQPV
VDLRTQKCYI TAQNHGYAVD SSSLPENWVP LMMNANDGTN EGIIHSSRPW FSVQFHPEAC
GGPTDTDFLF DYFLQFIAEP TASPVTTMPY SIPTVYRKVL VLGSGGLTIG QAGEFDYSGS
QAIKALKEAG IMSILINPNI ATVQTSAGMA DRVYFLPVTP DFVIKVIERE KPDGIFAAFG
GQTALNCAVK LHERGVFEKY NVKVLGTQIE AIMKTEDRDL FSKVVEACGE KIAESACCDC
VADAVEAATQ IGYPVLVRAA YALGGLGSGF ADNEEELRRL VNVALVNSPQ VIIDKSLKGW
KELEYEVVRD KNDNCITVCN MENFDPMGVH TGESIVIAPS QTLTNAEYYR LRQCALKVIR
HLGIVGECNI QYAVDTKTSE FRIIEVNARL SRSSALASKA TGYPLAYVAA KLALGHDLVQ
LRNSVTKCTT ACFEPSLDYC VAKVPRWDLQ KFSTVDARIG SAMQSVGEVM AIGRTFEETI
QKALRMVDDA SLGFDPIRYE LELGRRGLAT SGPNFDAELK KELANPTPVR MWAIAKAFEH
GMNVEEVHTL TNIDRWFLSK LHGLHMLKGT MKSLDFYALR QNPVLLKEAK TRGFSDKQIA
AIISAPEKII DSEISPHLLP SDHGSQRYSG GPVSEAHVRH LRKKLGIVPT VKQIDTLAAE
FPATTNYLYV TYSGDEHDLQ LAGSTKQCSD LPGTELISGY AIPEPLALNF QSSSDVMQQS
SKANKDVDAD SRIVVLGCGP YRIGSSVEFD WCSVNCIRTL RSLGHTAIVI NCNPETVSTD
FDESDRLYFE ELSHERVMDI AELEDPRGVV VSVGGQTPNN LALGLHKCGI RILGTSVEAI
DACEDRNKFS QLCDSLRIDQ PEWSQFATLQ EARQFCKAAG YPVLVRPSYV LSGAAMRVVT
NDGDLDLFLK TAAVVSRDHP VVISKYITGA KEVEMDGVGK SGDLVNYAIA EHVENAGVHS
GDATLLLPAQ RLFVETHRKV KSISQKLCRA LKISGPFNIQ FICKDNEVKV IECNLRASRS
MPFISKTYNV NFIELATRIM TGMPVHPAII QPMDIDFVAC KVPMFSFGRL KNSDPRLGVE
MSSTGEVACF GVNAYEAFLK GMMAANFKLP TKNILVSIGP AAAKAEFLAT GAAKQLQDMG
FTLFATKNTH EYLTNTGGLS CSLVYKPLIK REPNVLTMLQ TGKIDLVIDV PDSMDSDALT
DGFKIRRGAI EAAVSLITDI KTAIFTCSAL HRKWVAGPAA SAAQLAQIVA GLRDVKGLDP
KLQKRLYSIA AQSGGFVPLH GRLFAQFLHH AFPRDCPYPH EAGTTNPQTP DDWMRTKGRS
TTVSREQLEQ LARETCPADV HHGNAPSYCQ SEDADLPWSN SEDREHLLNM SRYGPPPKFA
ESPPELGFKV NSGIVPPSKL LAWLVTLPAF VAVAYTLGVL LGKTLLRRRY PAVVPAVAFL
WMAMVCVSLD LLDVRAAFGA GMIFLIWRIL VSRFLERPAG SKFADMVV
//
