ID A0A1S3MA18_SALSA Unreviewed; 2264 AA.
AC A0A1S3MA18;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=CAD protein-like isoform X1 {ECO:0000313|RefSeq:XP_014000033.1};
GN Name=LOC106571444 {ECO:0000313|RefSeq:XP_014000033.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014000033.1};
RN [1] {ECO:0000313|RefSeq:XP_014000033.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014000033.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001777};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001062};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58228; EC=2.1.3.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001363};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004812}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC {ECO:0000256|ARBA:ARBA00004852}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00004880}.
CC -!- SIMILARITY: In the 2nd section; belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00043998}.
CC -!- SIMILARITY: In the 3rd section; belongs to the metallo-dependent
CC hydrolases superfamily. DHOase family. CAD subfamily.
CC {ECO:0000256|ARBA:ARBA00043968}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the
CC aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
CC {ECO:0000256|ARBA:ARBA00043979}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the CarA family.
CC {ECO:0000256|ARBA:ARBA00043984}.
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DR RefSeq; XP_014000033.1; XM_014144558.1.
DR STRING; 8030.ENSSSAP00000108139; -.
DR PaxDb; 8030-ENSSSAP00000108139; -.
DR Ensembl; ENSSSAT00000142996; ENSSSAP00000108167; ENSSSAG00000074294.
DR GeneID; 106571444; -.
DR KEGG; sasa:106571444; -.
DR OMA; ENAAYYY; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000087266; Chromosome ssa15.
DR Bgee; ENSSSAG00000074294; Expressed in testis and 14 other cell types or tissues.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-EC.
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:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01316; CAD_DHOase; 1.
DR CDD; cd01744; GATase1_CPSase; 1.
DR CDD; cd01423; MGS_CPS_I_III; 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_00001; Asp_carb_tr; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
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; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
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; TIGR00670; asp_carb_tr; 1.
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; PF01979; Amidohydro_1; 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; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
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; SSF51338; Composite domain of metallo-dependent hydrolases; 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; PS00097; CARBAMOYLTRANSFERASE; 1.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
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:UP000087266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 517..709
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1053..1244
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1309..1465
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1818..1877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 252
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 336
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 338
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2264 AA; 250754 MW; AB29677EFE9FB7FF CRC64;
MATLILEDGT TFKGRLFGAN ASVSGEVVFQ TGMVGYPEAL TDPSYRCQIL TLTYPLQGNY
GIPQDEEGDF GLSKWFESSK IHAAALIVGE VSQNPSHWSS AMSLDQWLKE QGIPGLEGVD
TRSLTKKIRE KGTMLGKLVV DGTLEANVPF DNPDQRNLVK EVSMKVPLVF NPSGTVRITA
VDCGIKYNQI RCLCQRGACV TVVPWDHPLD STDFDGLFIS NGPGDPQFCK ETINNVRKVV
CVDNPKPVFG ICLGHQLLSL VIGAKTYKMK YGNRGHNQPC IHKGTDRCFI TSQNHGFAVD
PLTLPQGWDV LFTNANDQTS EGIVHNTKHL FSVQFHPEHM AGPTDLVSLF DVFLDTVRDH
KEGKSGKPVK QRLTEHLTYP GSPKPEEFVR PRKVLILGSG GLSIGQAGEF DYSGSQAIKA
LKEENIQTVL INPNIATVQT SKGLADKVYF LPLTPEYVTE VIKNERPDGV LLTFGGQTAL
NCGVELTKRG VLEKYAVRVL GTPVASIEMT EDRKIFVEKM EEINEHVAPS EAALSVEQAV
AAAERLGYPV LVRAAFALGG LGSGFANNSE ELTSLVTSAF AHTSQVLVDK SLKGWKEIEY
EVVRDAYDNC ITVCNMENID PLGIHTGESI VVAPSQTLND YEYNMLRDTA IKVIRHLGIV
GECNIQYALN PESEQYYIIE VNARLSRSSA LASKATGYPL AYVAAKLGLG IPLPVLKNSV
TNQTTANFEP SLDYCVVKVP RWDLSKFLRV STKIGSSMKS VGEVMAIGRS FEEAFQKALR
MVDENCVGFD HTIKPVSDEE LQTPTDKRIF VLAAALRAGY TVDRLYDLTK IDRWFLHKMK
NIADHEKVLE SYNQDESAMP LEVMRKAKQL GFSDKQIALA VQSTELAMRK LRHDWSILPV
VKQIDTVAAE WPAQTNYLYL TYNGTESDLG FSEPHVMVIG SGVYRIGSSV EFDWCAVGCI
MELRKMGYKT IMVNYNPETV STDYDMCDRL YFDEISFEVV MDIYEMENPE GVILSMGGQL
PNNIAMSLHR QQCRILGTSP EFIDSAENRF KFSRMLDTIG ISQPLWKELT AIESAMKFCE
TVGYPCLVRP SYVLSGAAMN VAYTDSDLEK YLSSAVAVSK EYPVVISKFI QEAKEIDVDA
VACDGVVMAI AVSEHVENAG VHSGDATLVT PAQDINQKTM ERIKVIVHAI GQELQVTGPF
NLQLIAKDDQ LKVIECNVRV SRSFPFVSKT LGVDLVALAT RVIMGEEVEP VGLMKGVGIV
GVKVPQFSFS RLAGADVVLG VEMTSTGEVA CFGENRYEAY LKAMLSTGFK IPKKNILLSI
GSYKNKSELL PTVQALESLG YDLYASLGTA DFYTEHGVKV MAVDWPFEEE ESDCPNKDKQ
RNILEYLEDH HFDMVINLSM RNSGGRRLSS FVTKGYRTRR MAIDYSVPLI IDIKCTKLFF
QALRLVGGFP PVKTHVDCMT SQKLIRLPGL IDVHVHLREP GATHKEDFSS GTAAALAGGV
TMVCAMPNTA PAIIDLSSLT MVQKLAKAGC RCDYALYVGA ALDNASVLPS IANSVAGLKM
YLNDTYSTLK MDNVSVWMEH FEKWPKHLPI VAHAEKQTVA AILMVAQLYQ RAVHICHVAK
KEEILIIRVA KQKGIQVTCE VAPHHLFLCE ENVADIGDGR AQVRPMLGTR EDMEALWENM
DIIDCFATDH APHSVEEKNS EKPPPGYPGL ETMMPLLLTA VSDGRLTVDD IIKRLYDNPR
KIFSLPAQDN TYVEVDLEQE WVIPKHMQFT KSKWTPFEGM KVKGKVRRVV LRGEVAYIDG
QVLVPPGYGE DVKTWPAPIP TQPPEPVKEV QQTPEHPRLT SPCEGIRTRA PSPRRSAGDG
RYMLPPRIHR SSDPGVTPGF RTIHTKWRLD FVAEDSRERA LRRAFEEDLK EEMAPVAGDG
SSHPPPLARV LSPRTEAGLG VAAGQPQTLT HLQTSPLLHP LVGQHILSVR QFSKEQISHL
FNVAHTLRLM IQKERTLDIL KGKVMASMFY EVSTRTSSSF AAAMQRLGGS VVHFCEATSS
SQKGESLADS VQTMSCYADV LVLRHPMPGA VESAARHCRK PVINAGDGVG EHPTQALLDV
FTIREELGTV NGMTITMVGD LKHGRTVHSL ARLLTQYRIT LRYVAPKNLH MPSEIIDFVA
SKGIKQEEFE SIEEALPDTD VLYITRIQKE RFSSEEEYKA CFGQFILTPH IMTGAKRKMV
VMHPLPRVNE ISAEVDTDPR AAYFRQAENG MYIRMALLAT VMGR
//
