CARA_ASPOR
ID CARA_ASPOR Reviewed; 450 AA.
AC Q2U913;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Carbamoyl-phosphate synthase arginine-specific small chain;
DE Short=CPS-A;
DE EC=6.3.5.5;
DE AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, glutamine chain;
GN Name=cpa1; ORFNames=AO090701000214;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1.
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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DR EMBL; AP007164; BAE61952.1; -; Genomic_DNA.
DR RefSeq; XP_001823085.1; XM_001823033.2.
DR AlphaFoldDB; Q2U913; -.
DR SMR; Q2U913; -.
DR STRING; 510516.Q2U913; -.
DR EnsemblFungi; BAE61952; BAE61952; AO090701000214.
DR GeneID; 5995142; -.
DR KEGG; aor:AO090701000214; -.
DR VEuPathDB; FungiDB:AO090701000214; -.
DR HOGENOM; CLU_035901_1_0_1; -.
DR OMA; CFNTGMT; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000006564; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 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 Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..450
FT /note="Carbamoyl-phosphate synthase arginine-specific small
FT chain"
FT /id="PRO_0000290589"
FT DOMAIN 220..407
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 296
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 380
FT /evidence="ECO:0000250"
FT ACT_SITE 382
FT /evidence="ECO:0000250"
SQ SEQUENCE 450 AA; 49118 MW; 4F52C179BA753038 CRC64;
MFAARLFKAM PARASAFPSV NASIQSRFMA TVRNGRVAHE RATFTIRDGP IFHGKSFGAR
SNISGEAVFT TSLVGYPESL TDPSYRGQIL VFTQPLIGNY GVPSAEKDQH GLLKYFESPH
LQAAGVVVAD VAEQYSHWTA VQSLGEWCAR EGVPAISGVD TRAIVTYLRE QGSSLARITV
GEEYDADQDE AFVDPEQIHL VRQVSTKAPF HVSAADPQCH VAVIDCGVKE NILRSLVSRG
ASITVFPYDY PIHKVAHHFD GVFISNGPGD PTHCQETAYH LRRLMETSQV PIFGICLGHQ
LLALAIGART IKLKYGNRAH NIPALDMSTG RCHITSQNHG YAVDASTLPS DWKPYFVNLN
DSSNEGMIHK TRPIFSTQFH PEAKGGPLDS SYLFDIYLDS VRKYKASQSA FHPTRDSLPS
PLLVDLLAKE RVGVQPTIGM QNVAAAAAAA
