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Database: UniProt
Entry: A0A0D2DEP7_9EURO
LinkDB: A0A0D2DEP7_9EURO
Original site: A0A0D2DEP7_9EURO 
ID   A0A0D2DEP7_9EURO        Unreviewed;       471 AA.
AC   A0A0D2DEP7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Carbamoyl-phosphate synthase arginine-specific small chain {ECO:0000256|ARBA:ARBA00040852};
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   ORFNames=Z517_10897 {ECO:0000313|EMBL:KIW76151.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW76151.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW76151.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW76151.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-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   -!- 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}.
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DR   EMBL; KN846975; KIW76151.1; -; Genomic_DNA.
DR   RefSeq; XP_013279959.1; XM_013424505.1.
DR   AlphaFoldDB; A0A0D2DEP7; -.
DR   STRING; 1442368.A0A0D2DEP7; -.
DR   GeneID; 25310387; -.
DR   VEuPathDB; FungiDB:Z517_10897; -.
DR   HOGENOM; CLU_035901_1_0_1; -.
DR   OrthoDB; 2783936at2759; -.
DR   Proteomes; UP000053029; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053029}.
FT   DOMAIN          51..190
FT                   /note="Carbamoyl-phosphate synthase small subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   ACT_SITE        307
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        391
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        393
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   471 AA;  51343 MW;  3999FB0B4AEFDB99 CRC64;
     MFSKALKQST LLPKAANIFS GASALRARSL ATVADNTTRQ QQFKSTTPTR ERATFTIRNG
     PIFDGVSFGA RSNVSGEAVF TTSLVGYPES LTDPSYRGQI LVFTQPLIGN YGVPSNARDE
     HGLLKYFESP NIQAVGVVVA DVAEKYSHWT AVESLSEWCA REGVPAISGV DTRAIVTFLR
     EQGSSLARIT IGEEYDADQD EAFIDPEQIN LVRKVSTKAP FHVSAASPNA HIAVLDCGVK
     ENILRSLVSR GASVTVFPFD YPIHKVAHHF DGVFISNGPG DPTHCQDTVY HLRKLMDSSQ
     IPIFGICLGH QLLALAAGAR TVKLKYGNRA HNIPALDLTT GKCHITSQNH GYAVDAATLP
     KGWKPYFLNL NDNSNEGLIH ESRPIFSTQF HPEAKGGPLD SSYLFDMYLD NVQKYKESQA
     ASQPYRDSKP SPLLVDLLAK ERVGVDLTQG IQNMMASTTQ EPERVYAAGA A
//
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