ID Q6CN46_KLULA Unreviewed; 2228 AA.
AC Q6CN46;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=KLLA0E15357p {ECO:0000313|EMBL:CAG99730.1};
GN ORFNames=KLLA0_E15357g {ECO:0000313|EMBL:CAG99730.1};
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590 {ECO:0000313|EMBL:CAG99730.1, ECO:0000313|Proteomes:UP000000598};
RN [1] {ECO:0000313|EMBL:CAG99730.1, ECO:0000313|Proteomes:UP000000598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC WM37 {ECO:0000313|Proteomes:UP000000598};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382125; CAG99730.1; -; Genomic_DNA.
DR RefSeq; XP_454643.1; XM_454643.1.
DR STRING; 284590.Q6CN46; -.
DR MEROPS; C26.956; -.
DR PaxDb; 284590-Q6CN46; -.
DR GeneID; 2893759; -.
DR KEGG; kla:KLLA0_E15357g; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_2_1_1; -.
DR InParanoid; Q6CN46; -.
DR OMA; WSPFNGK; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000598; Chromosome E.
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_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:UP000000598};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 560..752
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1097..1288
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1354..1505
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 300
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2228 AA; 246691 MW; 6247B216F40D1851 CRC64;
MSIITPTAPI TPPMESTGDR MITLELKDGT TLQGYSFGAE TTAAGELVFQ TGMVGYPESI
TDPSYEGQIL VITFPLVGNY GVPDRKLMDE YVEGLPRYFE SNRIHVAGLV IAHYTEEYSH
WLAQSSLGTW LKESNVPAVY GIDSRSLTKH LREAGSMLGR FALQKPGTSF EDANSAEWMS
YFETPEWVDP NVDNLVAKVS LKAPKLFVPN HPDIDLVQGP DGKTLRIVAV DVGMKYNQIR
CFVKRGVELL VVPWDYDFTT EEYDGLFISN GPGNPAILQE VSDRLTKVLD AKKTPVFGIC
LGHQLLARAS GASTLKMKFG NRGHNIPCTS TVSGRCYITS QNHGFAVDET SLTNGWKSLF
TNANDGSNEG IYHSELPYFS VQFHPESTPG PRDTEFLFDV FIQSVLDFKQ TGVLKQVEFP
GGNIEENLAA HPREDVKKVL VLGSGGLSIG QAGEFDYSGS QAIKALKEEG IYTILINPNI
ATIQTSKGLA DKVYFLPVTA EFVRKVILHE RPDAIYVTFG GQTALSVGIE MKDEFETLGV
KVLGTPIDTV ITTEDRELFA NAMDEINEKC AKSAAAATVA EALEAVKDIG FPVIVRAAYA
LGGLGSGFAS NEKELVDLCN VAFASSPQVL VERSMKGWKE IEYEVVRDAF DNCITVCNME
NFDPLGIHTG DSIVIAPSQT LSDEDYNMLR TTAVNVIRHL GVVGECNIQY ALNPTSKEYC
IIEVNARLSR SSALASKATG YPLAYTAAKL GLNIPLYEVK NSVTRSTCAC FEPSLDYCVV
KMPRWDLKKF TRVSTLLSSS MKSVGEVMSI GRTFEEAIQK AIRSTEYSNI GFSETDDELD
IDYELSNPSD MRIFAIANAF AKFGYSIDQV WEKTNIDKWF LNKLYSLIKF SDKISSYGSK
ENLPALVLKQ AKQLGFEDRQ IAKFLNSNEV AIRRLRKEYG IIPFVKQIDT VAAEFPAHTN
YLYLTYNAAA HDLDFNDHGV MVLGSGVYRI GSSVEFDWCA VTAVRTLRKN NFKTIMVNYN
PETVSTDYDE ADRLYFETIN LERIMDIYEL ESSAGVVVSM GGQTSNNIAM SLHRENVKIL
GTSPEMIDSA ENRYKFSRML DQIDVDQPAW KELTSMDEAE DFAEKVSYPV LVRPSYVLSG
AAMNTVYSKD DLESYLNQAV EVSREYPVVI TKYIENAKEI EMDAVALDGE LIMHVVSEHV
ENAGVHSGDA TLIVPPQDLD PETVRRIVEA TAKIGRALQI TGPYNIQFIA KNNEIKVIEC
NVRASRSFPF ISKVVGVNLI EMATKAIMGI PVTPYPVEKL PDDYVAIKVP QFSFPRLAGA
DPVLGVEMAS TGEVAAFGHS KYEAYLKSLL ATGFKLPKKN ILLSIGSYKE KQELLPGVKK
LYNMGYKLFA TAGTADFISE HGIPVQYLEV LNEEDDEKSE YSLTQHLANN KIDLYINLPS
ANRFRRPASY VSKGYRTRRM AVDFSVPLVT NVKCAKLLIE ALSRNMSLDV SERDAQTSHR
TVTIPGLINI SAYVPNISNV LLGPAELKEV TRLSVESGFT YSQIMPKSSS GPVITDAASL
KVANSVVKDS AYTNFGFTVA ATPNNIDTVS AVANEATSLF LPYRELSNNV PAVSEHLKHW
PLDKPVIAEA KTSDLASVIL LASLQNRSIH ITAVSNKEDL SLVMAVKEKQ SNVTCDVNIH
SLFVSQDDYP EAKFLPTKED QEFFWSNLES IDAFSIGSLP TALAAVTGNE IVTGLGIKEA
LPLLLSAVND GRLTIDDIVE RLHINPAKIF SIPEQNSAVE VDLDFTFRHT KRWSPYQKGG
LTGGIQRVLI NEETIVLSGD LVATEAKGQP ILPSKFTPTT PAVAKETPLA AVGTPILGAI
STSRKRFSFS NERRLSINSM DGDDEEAILD QPLEQRLMSS RPPKELSAPS VLINLIRTKN
PFLRRNILSV NQFKRSDFHA LFAVAQELRA GVEREGVLDV MKSRVLTTMF YEPSTRTSSS
FIAAMERLGG RTVNINTSAS SVKKGETLQD TIRTLACYSD AIVLRHPDEM SAHIAAKYSP
VPIINGGNGS REHPTQAFLD LFTIREELGT VNGITVTFMG DLKFGRPVHS LCRLLQHYQV
RINLIAPKEL RLPNALRKEL QDSGLLGIES ETLTPEIISK SDVLYCTRVQ QERFETEEDY
LKLKDTYIVD NKILSHAKQQ MVVMHPLPRV NEIREEVDYD HRAAYFRQMR YGLFVRMALL
AMVMGVEL
//
