ID A0A1G4KC19_9SACH Unreviewed; 2221 AA.
AC A0A1G4KC19;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=LAMI_0G14202g1_1 {ECO:0000313|EMBL:SCV01857.1};
GN ORFNames=LAMI_0G14202G {ECO:0000313|EMBL:SCV01857.1};
OS Lachancea mirantina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCV01857.1, ECO:0000313|Proteomes:UP000191024};
RN [1] {ECO:0000313|EMBL:SCV01857.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11717 {ECO:0000313|EMBL:SCV01857.1};
RA Devillers H.;
RL Submitted (MAR-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT598469; SCV01857.1; -; Genomic_DNA.
DR STRING; 1230905.A0A1G4KC19; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000191024; Chromosome g.
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; 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 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:UP000191024};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 562..754
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1099..1290
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1356..1506
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 1836..1861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1836..1860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 302
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 388
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2221 AA; 246002 MW; 097704AE43671AE3 CRC64;
MSIIVPTAPI TPPMESTGSR LFMLELQDGT SLQGYSFGAP VAAAGELVFQ TGMVGYPDSV
TDPSYEGQIL VITYPLVGNY GVPDRNLMDE YVETLPRYFE SNRIHIAGLV VAHYTEDYSH
WLAKSSLGAW LKEQCIPAVY GVDTRALTKH LRDAGSMLGR LALQKENSDA DRAASAEWRE
AFDVPDWIDP NVQNLVAKVS IKEPVLYEPP TDHEGITLQK GPDGKVLRIL VVDVGMKYNQ
IRCFVKRGVE LLVVPWDYDF TQDEYDGLFI SNGPGDPSVL SELTERLSIV IESKKSPIFG
ICLGHQLLAR ASGASTLKLK FGNRGQNIPC TSAISGKCYI TSQNHGFAVD VNSLTEGWKP
LFTNANDGSN EGIYNTKLPY FSVQFHPEST PGPRDTEFLF DVFIKSVKDF KFNKQLKAVE
FPGGKIDENL TAHPRVEAKK VLVLGSGGLS IGQAGEFDYS GSQAIKALKE EGIYTILINP
NIATIQTSKG LADKVYFLPV TPEFVRKVIL HERPDAIYVT FGGQTALSVG IAMKDEFETL
GVKVLGTPID TVITTEDREL FANAMDEINE KCAKSKAAAS VQEALDAVKD IGYPVIVRAA
YALGGLGSGF ASNDKELVDL CNIAFASSPQ VLVERSMKGW KEVEYEVVRD AFDNCITVCN
MENFDPLGIH TGDSIVVAPS QTLSDEDYNM LRTTAVNVIR HLGVVGECNI QYALNPFSKE
YCIIEVNARL SRSSALASKA TGYPLAYTAA KLGLNIPLNE VRNSVTQSTC ACFEPSLDYC
VVKMPRWDLK KFTRVSTQLS SSMKSVGEVM SVGRTFEEAM QKAIRSTEYA NLGFNETEGD
LDIDYELTHP SDMRIFAIAN AFSKLDYSVE KVWSMTNIDK WFLNKLYDLI QFVRKIESYS
VKENLPFALL KQAKQLGFDD RQIAKFLNSN EVAIRRLRKE HGIVPFVKQI DTVAAEFPAH
TNYLYMTYNA AAHDLDFNDH GVMVLGSGVY RIGSSVEFDW CAVTAVRTLR KNNIKTIMVN
YNPETVSTDY DEADRLYFET INLERVLDIY EAETSAGVVV SMGGQTSNNI AMSLHRENVK
ILGTTPEMID SAENRYKFSR MLDQIGVDQP AWKELTSIDE AESFAENVGY PVLVRPSYVL
SGAAMNTVYS KDDLASYLNQ AVEVSRDYPV VITKYIENAK EIEMDAVAKD GELVMHVVSE
HVENAGVHSG DATLIVPPQD LDPETVNRIV VATAKIATAL KITGPMNIQF IAKNNDIKVI
ECNVRASRSF PFISKVVGVN LIEMATEAVV GLPVKPYPTE KLPDDYVAIK VPQFSFPRLA
GADPVLGVEM ASTGEVACFG HSKYEAYLKS LLSTGFKLPK KNILLSIGSF KEKQEMLPSV
KKLYNLGFKL FATAGTADFI SEHGIPVQYL EVLSEGDEKS EYSLTQHLAN NKIDLYINLP
SANRFRRPAS YVSKGYRTRR MAVDYSVPLV TNVKCAKLLI EALSRHLQLD VSERDAQTSH
RTVTIPGLIN VSAYIPNVSN VVKGPAEMKE ITRVSAESGF TYSQIMPKST RGPVITNEKS
LAAARSVVKD SAYTDFAFTV AATAHNLNEI AECAQEANAL FIPYRELSNK VSMVADHLKN
WPVEKQVIAE AKTSDLASVI LLASLQNRAI HITGVCHKDD LALIKTVKEK QSKVTCDVNV
HALFVSQEDY PEALFLPTLE DQEFLWNNLD VIDAFSVGSL PTALADVTGN KVVTGIGIKE
ALPLLLSAVN EGKLSIDDIV ERLHDNPAQI FNIPKQNAVV EIDLDFTFRH TKRWSPYTKG
GLTGGVERVL VNDETIVLSG DLVTAEANGK SLTNTLSKQS LTTSTPSAET PTPFSSSRKR
FSFSNEKRSS VAAIEDDEEA LLDQPLEQRL MSSRPPKELA APGAIYSLIR GNNPFLRRNI
LSVNQFKRSD FHALFAVAQE LRSAVEREGV LDIMKGRVLT TLFYEPSTRT SSSFIAAMER
LGGRTVNVNT TSSSVKKGET LQDTIRTMAC YSDAIVLRHH DEMSAHTAAK YSPVPILNGG
NGSREHPTQA FLDLFTIREE LGTVNGITVT FMGDLKYGRP VHSLCRLLRH YQVRINLVSP
NELRLPQALR KELSNAGLLG VESEILTPDI ISRSDVLYCT RVQQERFEHP EEYERLKDVY
IVDNKILSHA KDHMVVMHPL PRVNEIREEV DYDHRAAYFR QMRYGMFVRM ALLAMVMGVD
L
//
