ID A0A1G4MH55_LACFM Unreviewed; 2219 AA.
AC A0A1G4MH55;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=LAFE_0G05688g1_1 {ECO:0000313|EMBL:SCW03222.1};
GN ORFNames=LAFE_0G05688G {ECO:0000313|EMBL:SCW03222.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW03222.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|EMBL:SCW03222.1, ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 6772 {ECO:0000313|EMBL:SCW03222.1};
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}.
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DR EMBL; LT598486; SCW03222.1; -; Genomic_DNA.
DR STRING; 4955.A0A1G4MH55; -.
DR OMA; WSPFNGK; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000190831; 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:UP000190831};
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 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 2219 AA; 245426 MW; DE763603FB038336 CRC64;
MSIVTPTGPV TPPMESTGDK LITLELQDGT VVQGYSFGAE VPAAGELVFQ TGMVGYPESI
TDPSYEGQIL VITFPLVGNY GVPDRNLKDE FVESLPRYFE SNRIHIAGLV IAHYTEEYSH
WLAKSSLGAW LKEENIPAVY GVDTRNLTKH LRDSGSMLGR LALQKEGTSF STATSAEWRE
AFEVPEWVDP NVQNLVAKVS VKEPTLYVPP TDHEGVNLQK GPDGKVLRIV AVDVGMKYNQ
IRCFVKRGVE LLVVPWDYDF TKEEYDGLFI SNGPGDPSVL SELSARLSAV LESKKTPVFG
ICLGHQLLAR ASGASTLKLK FGNRGHNIPC TSTISGKCYI TSQNHGFAVD VNTLTSGWKP
LFVNANDESN EGIYNVDLPY FSVQFHPEST PGPRDTEFLF DVFIKAVKEH KFTGQLKPVE
FPGGKIEENL AAFPRVEAKK VLVLGSGGLS IGQAGEFDYS GSQAIKALKE EGIYTILINP
NIATIQTSKG LADKVYFLPV TAEFVRKVIL HERPDAIYVT FGGQTALSVG IEMKDEFETL
GVKVLGTPID TIITTEDREL FANSMDSINE KCAKSQAASS TEEALAAVKD IGYPVIVRAA
YALGGLGSGF ASNDQELVEL CNVAFASSPQ VLVERSMKGW KEVEYEVVRD AFDNCITVCN
MENFDPLGIH TGDSIVVAPS QTLSDEDYNM LRTTAVNVIR HLGVVGECNI QYALNPFSKE
YCIIEVNARL SRSSALASKA TGYPLAYTAA KLGLNIPLNE VRNSVTQSTC ACFEPSLDYC
VVKMPRWDLK KFSRVSTQLS SSMKSVGEVM SIGRTFEEAI QKAIRSTEYA NLGFNETDIE
LDIDYELTHP SDMRIFAVAN AFAKLNYSID KVWQLTNIDK WFLNKLHDLV KFAQKIENYG
SKENLPALVL KQAKQLGFDD RQIAKFLNSN EVAIRRLRKD FGIVPFVKQI DTVAAEFPAH
TNYLYMTYNA AAHDLAFEDH GVMVLGSGVY RIGSSVEFDW CAVTAVRTLR KNDIKTIMIN
YNPETVSTDY DEADRLYFET INLERILDIY EIENSAGVVV SMGGQTSNNI AMSLHRENVK
ILGTTPEMID SAENRYKFSR MLDQIGVDQP AWKELTSMDE AEDFANKVGY PVLVRPSYVL
SGAAMNTVYS KDDLASYLNQ AVEVSRDYPV VITKYIENAK EIEMDAVAKD GELVMHVVSE
HVENAGVHSG DATLIVPPQD LDPETVNRIV VATAKIGKAL KITGPYNIQF IAKNNDIKVI
ECNVRASRSF PFISKVVGVN LIEMATKAIM GLPLTPYPTE KLPEDYVAIK VPQFSFPRLA
GADPVLGVEM ASTGEVATFG HSKYEAYLKS LLATGFKMPK KNILLSIGSF KEKQEMLPSV
KKLYNMGFKL FATAGTADFI SEHGIPVQYL EVLSEGDEKS EYSLTQHLAN NKIDLYINLP
SANRFRRPAS YVSKGYRTRR MAVDYSVPLV TNVKCAKLLV EALSRNLTLD VSERDAQTSH
RTVTIPGLIN ISSYIPNISN AVKGPAEMKE VTRLLVESGF TYSQIMPKST SGPVITDEQY
LKVANSVVKD SAYTDFGFTV AATANNVDDV ARCAKDANAL FLPYRELSNK VSIVAEHLKN
WPIEKQVIAE AKTSDLASVI LLASLQNRAI HITGVSNKDD LALIMTVKEK QTKVTCDVNI
HSLFVSQDDY PEALFLPTPE DQDFFWRNLD GIDAFSIGSL PTALANVTGN KVVTGLGIKE
ALPLLLSAVN SGKITIDDIV ERLHDNPAKI FNIPEQNAVV EIDLDFTFRH KKRWTPYTKG
GLTGGVERVL VNDETVVLSG DLVATEAKGQ PVVNSAKIAT PAPPAASELS HVTGSRKRFS
FSNEKRASIT SVEDEEEAII DQPLEQRLMS SRPPKELAAP GAIYSLIRGN NPFLRRNILS
VNQFRRSDFH ALFAVAQELR SAVEREGVLD IMKGRVLTTI FYEPSTRTSS SFIAAMERLG
GRTVNINTSS SSVKKGETLQ DTIRTLACYS DAIVMRHPDE MSAHTAAKYS PVPIVNGGNG
SREHPTQAFL DLFTIREELG TVNGITVTFM GDLKYGRPVH SLCRLLQHYQ VRINLVSPSE
LRLPQALRKE LSDAGMLGVE SETLTPEIIS KSDVLYCTRV QQERFDSKEQ YERLKDVYIV
DNKILSHAKD QMVVMHPLPR VNEIREEVDY DHRAAYFRQM RYGLFVRMAL LAMVMGVDL
//
