ID A0A168IKZ2_MUCCL Unreviewed; 2216 AA.
AC A0A168IKZ2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAD00066.1};
GN ORFNames=MUCCIDRAFT_74513 {ECO:0000313|EMBL:OAD00066.1};
OS Mucor lusitanicus CBS 277.49.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=747725 {ECO:0000313|EMBL:OAD00066.1, ECO:0000313|Proteomes:UP000077051};
RN [1] {ECO:0000313|EMBL:OAD00066.1, ECO:0000313|Proteomes:UP000077051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAD00066.1,
RC ECO:0000313|Proteomes:UP000077051};
RG DOE Joint Genome Institute;
RA Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA Gabaldon T., Grigoriev I.V.;
RT "Expansion of signal transduction pathways in fungi by whole-genome
RT duplication.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- 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}.
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:OAD00066.1}.
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DR EMBL; AMYB01000007; OAD00066.1; -; Genomic_DNA.
DR STRING; 747725.A0A168IKZ2; -.
DR VEuPathDB; FungiDB:QYA_74513; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000077051; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:InterPro.
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; 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; 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; 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; 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; 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; 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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
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:UP000077051};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 619..811
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1156..1347
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1413..1563
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 359
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 443
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2216 AA; 243363 MW; EBD785C4BC859FD9 CRC64;
MSSNFPIPSV AAAGTAPAIT SSVGGAHIPA PAANATPLPA LSPRSPSAPH RPVTAFEDKD
VTTATLVLQD GSSYQGISFG AEGKSISGEC VFQTGMVGYP ESLTDPSYRG QILVLTFPLV
GNYGVPSRIE MDELLKDIPK YFESSEIHVA GLIVGNYAQD YSHYLATSSL SAWLKENSVP
GLYGIDTRAM TKKIRTKGAL LGKILFPKSL ANSTVDAAAS ALGLSAASNL MPSERWMVDY
QDVDWVDPNK RNLVAEVSIK EPKIYYPDPA KAIKTPSGRT MRIIAVDIGM KYNQIRCFVF
RGVELKIVPW DYDFNAEPAD SYDGLFLSNG PGDPTTIDIT IKNTAKFLTD LKKPVFGICL
GHQVMALAAG AKTMKMKYGN RGQNIPCTNM LSGRCYITSQ NHGYAVDAAS LPEHYQELFV
NANDGSNEGV IHKSLPIFSV QFHPESTPGP RDTEFLFDVF LGNVKDCLEK NTLVPVQMPG
GDIVENRNKN PRVHVNKVLV LGSGGLSIGQ AGEFDYSGSQ AIKALKEEGI YTVLINPNIA
TIQTSKGLAD KVYFLPVTPE YVRKVIQFEK PDGIYVTFGG QTALSVGIAL KDEFEGLGVK
VLGTSIDTVI TTEDRDLFAQ ALYEINEKCA QSSSAVTVDE AVAAAKEIGY PVICRAAYAL
GGLGSGFADN EKELVALCNK AFATSPQVLI EKSMKGWKEI EYEVVRDCQD NCITVCNMEN
FDPLGIHTGD SIVIAPSQTL SDEDYNMLRT TAVNVIRHLG VVGECNIQYA LNPFSKEYCI
IEVNARLSRS SALASKATGY PLAFVAAKLG LGIPLNEIKN SVTKVTCACF EPSLDYVVVK
IPRWDLKKFN RVSTALSSSM KSVGEVMAIG RTFEETIQKA IRAIDFNFVG FSENEFVAAE
DIDFELTNPS DQRLFAIANA MNKGYTVDKI WEMTKIDKWF LNKLMHIVNL GGRLNGFNKS
NVPGNLIRSA KQLGFSDRQI ASHINSNELA VRRLRQEYGV TPFVKQIDTV AAEFPAFTNY
LYMTYNAVEH DIEFEDKGIM VLGSGVYRIG SSVEFDWCAV RAIRTIREQG LKTVMVNYNP
ETVSTDYDEA DRLYFENINL ERILDIYEIE KSSGVLMSMG GQTPNNIALP LYRQNVKVLG
TSPEMIDNAE NRYKFSRMCD SIGVDQPLWK ELTSYEEAEV FCENVGFPVL VRPSYVLSGA
AMNVVFSKDD LASYLKEAAA VSRDHPVVIT KYIEEAKEVD MDAVALDGKL VMHVISEHVE
NAGVHSGDAT LVLPPQDLDP ETIRKIEVAT AKIGRALNIT GPFNIQFIAK NNEIKVIECN
VRAARSSPFV SKVMGVDLIE MATLAMLGLP VTPYPKVEIP KDYVGVKVPQ FSFSRLSGAD
PVLGVEMAST GEVACFGKDK FSAYLKALLA TGLTLPKKNI LFSIGSYKEK QELLPSVRKL
HQLGYNIFAT TGTADFISEH NIPVKHLDTL DADTDDKLKA EYSLQQHLSN NLIDLYINLP
SRNRFRRPAS YMSKGYRSRR MAVDYSVPLL TNVKCAKLFI EALARNKDNE ILSIDCKSSH
TQAHLPGLFN MNAYLESSDE FAAVAKASLS AGFTTVSAFA KDVTNDITLD KLSDMARKEA
YTDYLLNITA TADNAAQVGD YASDAAAVYL NTDRIGSGKV SVFDSAFSSW PRSQLIVTDA
KGTDLASLLL LASLHNRVIH VSNVASKADL ALIKMSKKKG MSITCDVAIY SLFFHSEEFE
NTKLLPTKKE QEALWRNLNV IDCFTIGSVP RKLAAELGQP ADATAGIHEA LPLLLGAVSQ
GRLTISDVSE RLYDNPRAIF GISAQPDTSI ELVVDRKIKW PVDNENWSPI AGRTVHGSVE
RVVMDETTMF MDGSFMEGGA KLGRDQLVSL QAPSFEISAS LARVVSRSPF YRKHILRSAQ
FDRDDLHLLF GVAHEMRNLV ELYGSINLLQ GRVMSTMFFE PSTRTSSSFE AAMYRLGGQV
VSVSATTSSV QKGESLADTV RTLGCYADLI VLRHPQPGSA QIAAKYSKVP VINAGDGIGE
HPTQAFLDTF TIREELGTVN GLTITLVGDL KNGRTVHSLV KILTYYQVTI NYVCPDSLAM
PKDVMEEVAA AGIKQNVCSS LDEVIGTTDV LYMTRVQKER FDTEEEYRRV KDAYILNNDV
LSKAKSQMIV MHPLPRVNEI EPEVDFDQRA AYFRQMRYGL FVRMALLALV MGTHRG
//
