ID   CARA_EMENI              Reviewed;         454 AA.
AC   Q5BB37; C8VMT6; O42806;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 2.
DT   25-MAY-2022, entry version 102.
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=cpa-1; ORFNames=AN2243;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-304.
RA   Doonan J.;
RT   "A CPA-like gene from Aspergillus nidulans.";
RL   Submitted (MAR-1998) 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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA63928.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AACD01000036; EAA63928.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001307; CBF86449.1; -; Genomic_DNA.
DR   EMBL; AJ224085; CAA11831.1; -; mRNA.
DR   RefSeq; XP_659847.1; XM_654755.1.
DR   AlphaFoldDB; Q5BB37; -.
DR   SMR; Q5BB37; -.
DR   STRING; 162425.CADANIAP00008930; -.
DR   EnsemblFungi; CBF86449; CBF86449; ANIA_02243.
DR   EnsemblFungi; EAA63928; EAA63928; AN2243.2.
DR   GeneID; 2875485; -.
DR   KEGG; ani:AN2243.2; -.
DR   VEuPathDB; FungiDB:AN2243; -.
DR   eggNOG; KOG0370; Eukaryota.
DR   HOGENOM; CLU_035901_1_0_1; -.
DR   InParanoid; Q5BB37; -.
DR   OMA; CFNTGMT; -.
DR   OrthoDB; 566537at2759; -.
DR   UniPathway; UPA00068; UER00171.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW   Glutamine amidotransferase; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..454
FT                   /note="Carbamoyl-phosphate synthase arginine-specific small
FT                   chain"
FT                   /id="PRO_0000290595"
FT   DOMAIN          219..406
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        295
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        379
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000250"
FT   CONFLICT        14
FT                   /note="A -> P (in Ref. 3; CAA11831)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  49638 MW;  050C58FFCF9F4AD9 CRC64;
     MMFSRFFKAV PARAPAFSSP LPVYQARTMA TVRNQRPVER ATFTIRDGPI FHGKSFGART
     TISGEAVFTT SLVGYPESLT DPSYRGQILV FTQPLIGNYG VPSTERDRHG LLKYFESPNL
     QAAGVVVADV AEQYSHWTAV QSLGEWCARE GVPAISGVDT RAIVTYLREQ GSSLARITVG
     EEYDADQDEA FTDPEQIHLV RQVSTKAPFH VSAADPQCHV AVLDCGVKEN ILRSLVSRGA
     SITVFPFDYP IHKVAHHFDG VFISNGPGDP THCQDTTYHL RRLMETSQVP IFGICLGHQL
     LALAAGARTV KLKYGNRAHN IPALDLTTGR CHITSQNHGY AVDASTLPSD WKPYFVNLND
     SSNEGMIHKS RPIFSTQFHP EAKGGPLDSS YLFDIYIDSV KKYKNSQLAF HPSRETIPSP
     LLVDLLPKER VDVAPTIGMQ NVAAAAAAAA AATA