GenomeNet

Database: UniProt
Entry: E6R5Y6_CRYGW
LinkDB: E6R5Y6_CRYGW
Original site: E6R5Y6_CRYGW 
ID   E6R5Y6_CRYGW            Unreviewed;       446 AA.
AC   E6R5Y6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012738};
DE            EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE   AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, glutamine chain {ECO:0000256|ARBA:ARBA00042128};
GN   OrderedLocusNames=CGB_D3280C {ECO:0000313|EMBL:ADV21740.1};
OS   Cryptococcus gattii serotype B (strain WM276 / ATCC MYA-4071)
OS   (Filobasidiella gattii) (Cryptococcus bacillisporus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus gattii species complex.
OX   NCBI_TaxID=367775 {ECO:0000313|EMBL:ADV21740.1, ECO:0000313|Proteomes:UP000007805};
RN   [1] {ECO:0000313|EMBL:ADV21740.1, ECO:0000313|Proteomes:UP000007805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM276 / ATCC MYA-4071 {ECO:0000313|Proteomes:UP000007805};
RX   PubMed=21304167; DOI=10.1128/mBio.00342-10;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwon-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 2:E342-E342(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WM276;
RA   D'Souza C.A., Kronstad J.W., Taylor G., Warren R., Yuen M., Hu G.,
RA   Jung W.H., Sham A., Kidd S.E., Tangen K., Lee N., Zeilmaker T., Sawkins J.,
RA   McVicker G., Shah S., Gnerre S., Griggs A., Zeng Q., Bartlett K., Li W.,
RA   Wang X., Heitman J., Stajich J.E., Fraser J.A., Meyer W., Carter D.,
RA   Schein J., Krzywinski M., Kwong-Chung K.J., Varma A., Wang J., Brunham R.,
RA   Fyfe M., Ouellette B.F.F., Siddiqui A., Marra M., Jones S., Holt R.,
RA   Birren B.W., Galagan J.E., Cuomo C.A.;
RT   "Genome variation in Cryptococcus gattii, an emerging pathogen of
RT   immunocompetent hosts.";
RL   MBio 0:0-0(2011).
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   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by the
CC       large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000256|ARBA:ARBA00011275}.
CC   -!- SIMILARITY: Belongs to the CarA family.
CC       {ECO:0000256|ARBA:ARBA00007800}.
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; CP000289; ADV21740.1; -; Genomic_DNA.
DR   RefSeq; XP_003193527.1; XM_003193479.1.
DR   AlphaFoldDB; E6R5Y6; -.
DR   GeneID; 10191176; -.
DR   KEGG; cgi:CGB_D3280C; -.
DR   VEuPathDB; FungiDB:CGB_D3280C; -.
DR   eggNOG; KOG0370; Eukaryota.
DR   HOGENOM; CLU_035901_1_0_1; -.
DR   OrthoDB; 2783936at2759; -.
DR   Proteomes; UP000007805; Chromosome D.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01744; GATase1_CPSase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR   HAMAP; MF_01209; CPSase_S_chain; 1.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR035686; CPSase_GATase1.
DR   InterPro; IPR017926; GATASE.
DR   NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR   PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          42..181
FT                   /note="Carbamoyl-phosphate synthase small subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   ACT_SITE        300
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        394
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        396
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   446 AA;  48465 MW;  9E90689BD5741C7B CRC64;
     MSAIRAINMR KTASALKAPI AFKRTLATPV NSLYTPILPA KIPATLHLKS GQSYYGSSFG
     SENSKFGETV FSTSITSYTD SMTDPSYLGQ ILVFTSPMIG NYGVPSNVSS QFPGIPFLES
     EKIQCTGVVV SDVALKYSHY QAVESLHEWC KRYDVPGITG VDTRAITSLL RDQGTTLGRL
     AVGDEAGKPA PQESEYWDPS KENLVAQAST KKPYVLNEKG SGPRIAVFDF GIKANILRSL
     VRRDAVVTVL PWDFDFNAVR DQFDGLFLSN GPGDPKMIMD TAMRIRQTIN EWDKPIFGIC
     MGHQVLGLAA GLEAYRMTFG NRGHNQPVLA LASSGSIKAG RVYVTSQNHQ YALRLTEDFP
     EGWAPFFINC NDSSVEGIIS TPESGKRIWG VQFHPESAGG PLDTIEMFSD FVNECDVGRK
     GFNASAMVAN EVKVDGHAAK AASVSA
//
DBGET integrated database retrieval system