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   16-JUN-2009, entry version 19.
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 / FGSC A1164 / NRRL
OS   181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Neosartorya.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P.,
RA   Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A.,
RA   Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A.,
RA   Galens K., Fraser-Liggett C.M., Haas B.J., Inman J.M., Kent R.,
RA   Lemieux S., Malavazi I., Orvis J., Roemer T., Ronning C.M.,
RA   Sundaram J.P., Sutton G., Turner G., Venter J.C., White O.R.,
RA   Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., Wortman J.R.,
RA   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: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from HCO(3)(-): 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
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the carA family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DS027686; EAW24062.1; -; Genomic_DNA.
DR   RefSeq; XP_001265959.1; -.
DR   GeneID; 4592759; -.
DR   KEGG; nfi:NFIA_036340; -.
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-hyd...; IEA:EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006220; Anth_synthII.
DR   InterPro; IPR001317; CarbamoylP_synth_GATase.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR011702; GATASE.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   PANTHER; PTHR11405:SF4; CarA_synth_small; 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   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Cytoplasm; Glutamine amidotransferase; Ligase;
KW   Nucleotide-binding.
FT   CHAIN         1    453       Carbamoyl-phosphate synthase arginine-
FT                                specific small chain.
FT                                /FTId=PRO_0000290597.
FT   DOMAIN      219    406       Glutamine amidotransferase type-1.
FT   COMPBIAS    443    453       Poly-Ala.
FT   ACT_SITE    295    295       Nucleophile (By similarity).
FT   ACT_SITE    379    379       By similarity.
FT   ACT_SITE    381    381       By similarity.
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
//