ID   CARA_NEOFI              Reviewed;         453 AA.
AC   A1CZ92;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 91.
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=NFIA_036340;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027686; EAW24062.1; -; Genomic_DNA.
DR   RefSeq; XP_001265959.1; XM_001265958.1.
DR   AlphaFoldDB; A1CZ92; -.
DR   SMR; A1CZ92; -.
DR   STRING; 36630.CADNFIAP00003433; -.
DR   EnsemblFungi; EAW24062; EAW24062; NFIA_036340.
DR   GeneID; 4592759; -.
DR   KEGG; nfi:NFIA_036340; -.
DR   VEuPathDB; FungiDB:NFIA_036340; -.
DR   eggNOG; KOG0370; Eukaryota.
DR   HOGENOM; CLU_035901_1_0_1; -.
DR   OMA; CFNTGMT; -.
DR   OrthoDB; 566537at2759; -.
DR   UniPathway; UPA00068; UER00171.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
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..453
FT                   /note="Carbamoyl-phosphate synthase arginine-specific small
FT                   chain"
FT                   /id="PRO_0000290597"
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"
SQ   SEQUENCE   453 AA;  49347 MW;  549077BF63DB7BFF CRC64;
     MFARVFKAMP ARASALTSVN ASIQARFMAT VRQQRTAHER ATFTIRDGPI FHGKSFGART
     NISGEAVFTT SLVGYPESLT DPSYRGQILV FTQPLIGNYG VPSAERDQHG LLKYFESPNL
     QAAGVVVADV AEQYSHWTAV ESLGEWCARE GVPAISGVDT RAIVTYLREQ GSSLARITVG
     EEYDADQDEA FTDPEQIHLV RQVSTKAPFH VSAADPQCHV AVIDCGVKEN ILRSLVSRGA
     SITVFPFDYP IHKVAHHFDG VFISNGPGDP THCQETTYHL RRLMETSQVP IFGICLGHQL
     LALAAGARTI KLKYGNRAHN IPALDLSTGR CHITSQNHGY AVDASTLPSD WKPYFVNLND
     SSNEGMIHKS RPIFSTQFHP EAKGGPLDSS YLFDIYIDSV KKYKASQAAF HPQRDSLPSP
     LLVDLLAKER VGVQPTIGMQ NIAAAATAAA AAA