(data stored in SCRATCH zone)

HOGENOM: FUNUC1_1_PE1001

ID   FUNUC1_1_PE1001                      STANDARD;      PRT;   358 AA.
AC   FUNUC1_1_PE1001; Q8RG87;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Carbamoyl-phosphate synthase small chain; EC=6.3.5
DE   5;AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
DE   (FUNUC1_1.PE1001).
GN   Name=carA; OrderedLocusNames=FN0421;
OS   FUSOBACTERIUM NUCLEATUM SUBSP. NUCLEATUM ATCC 25586.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FUNUC1_1.PE1001.
CC       Fusobacterium nucleatum subsp. nucleatum ATCC 25586 chromosome, complet
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:CARA_FUSNN
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 bicarbonate: step 1/1.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
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   -!- SIMILARITY: Belongs to the CarA family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC   -!- GENE_FAMILY: HOG000038087 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8RG87; -.
DR   EMBL; AE009951; AAL94624.1; -; Genomic_DNA.
DR   RefSeq; NP_603325.1; NC_003454.1.
DR   ProteinModelPortal; Q8RG87; -.
DR   GeneID; 991442; -.
DR   GenomeReviews; AE009951_GR; FN0421.
DR   KEGG; fnu:FN0421; -.
DR   NMPDR; fig|190304.1.peg.1004; -.
DR   OMA; YESIAPT; -.
DR   ProtClustDB; PRK12564; -.
DR   BioCyc; FNUC190304:FN0421-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; 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   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01209; CPSase_S_chain; 1; -.
DR   InterPro; IPR006220; Anth_synthII.
DR   InterPro; IPR001317; CarbamoylP_synth_GATase_dom.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR011702; GATASE.
DR   InterPro; IPR017926; GATASE_1.
DR   Gene3D; G3DSA:3.50.30.20; G3DSA:3.50.30.20; 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   SUPFAM; SSF52021; CP_synthsmall; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   HOGENOMDNA; FUNUC1_1.PE1001; -.
KW   carbamoyl phosphate synthase small subunit;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Glutamine amidotransferase; Ligase;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome.
SQ   SEQUENCE   358 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MYNRQLILED GTVYKGYAFG ADVENVGEVV FNTSMTGYQE ILSDPSYNGQ IVTLTYPLIG
     NYGINRDDFE SMKPCIKGMV VKEVCATPSN FRSEKTLDEA LKDFGIPGIY GIDTRALTRK
     LRSKGVVKGC LVSIDRNVDE VVAELKKTVL PTNQIEQVSS KSISPALGRG RRVVLVDLGM
     KIGIVRELVS RGCDVIVVPY NTTAEEVLRL EPDGVMLTNG PGDPEDAKES IEMIKGIINK
     VTIFGICMGH QLVSLACGAK TYKLKFGHRG GNHPVKNILT GRVDITSQNH GYAVDIDSLN
     DTDLELTHIA INDRSCEGVR HKKYPVFTVQ FHPEAAAGPH DTSYLFDEFI KNIDNNMK
//

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