CARA_NEIGO
ID CARA_NEIGO Reviewed; 377 AA.
AC Q50983; Q59598;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000255|HAMAP-Rule:MF_01209};
DE EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01209};
DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000255|HAMAP-Rule:MF_01209};
GN Name=carA {ECO:0000255|HAMAP-Rule:MF_01209};
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MS11;
RA Rudel T., Boxberger H.J., Pandit J., Meyer T.F.;
RT "The Neisseria gonorrhoae carA gene: generation of mutants and implication
RT of pyrimidine biosynthesis for the infection of epithelial cells.";
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CH811;
RX PubMed=7773412; DOI=10.1099/13500872-141-5-1183;
RA Lawson F.S., Billowes F.M., Dillon J.A.;
RT "Organization of carbamoyl-phosphate synthase genes in Neisseria
RT gonorrhoeae includes a large, variable intergenic sequence which is also
RT present in other Neisseria species.";
RL Microbiology 141:1183-1191(1995).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01209};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01209}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC Rule:MF_01209}.
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 -!- SIMILARITY: Belongs to the CarA family. {ECO:0000255|HAMAP-
CC Rule:MF_01209}.
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DR EMBL; Z54242; CAA91011.1; -; Genomic_DNA.
DR EMBL; U11295; AAA74995.1; -; Genomic_DNA.
DR AlphaFoldDB; Q50983; -.
DR SMR; Q50983; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Pyrimidine biosynthesis.
FT CHAIN 1..377
FT /note="Carbamoyl-phosphate synthase small chain"
FT /id="PRO_0000112297"
FT DOMAIN 190..377
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT REGION 1..186
FT /note="CPSase"
FT ACT_SITE 266
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT ACT_SITE 350
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT ACT_SITE 352
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT CONFLICT 63
FT /note="T -> A (in Ref. 2; AAA74995)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..77
FT /note="SVYA -> TVLP (in Ref. 2; AAA74995)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="Missing (in Ref. 2; AAA74995)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..208
FT /note="MLAS -> ISP (in Ref. 2; AAA74995)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..238
FT /note="NG -> QR (in Ref. 2; AAA74995)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="G -> A (in Ref. 2; AAA74995)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="S -> F (in Ref. 2; AAA74995)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="S -> F (in Ref. 2; AAA74995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 40515 MW; BD54FAF60506BCA2 CRC64;
MNTPALLVLA DGSVFHGTSI GYEGSASGEV VFNTSMTGYQ EILTDPSYCK QIVTLTYPHI
GNTGTNAEDE ESRSVYAAGL IIRDLPLLHS NFRASESLHD YLVRNETVAI ADIDTRRLTM
LLREKGAQGG AILTGADATV EKAQELIAAF GSMVGKDLAK EVSCTETYEW TEGEWELGKG
FVTPDKQPYH VVAYDFGVKT NILRMLASRG CRLTVVPAQT SAEDVLALNP DGVFLSNGPG
DPEPCTYGIE AVQKLMESGK PIFGICLGHQ LISLAIGAKT LKMRFSHHGA NHPVQDLDSG
KVVITSQNHG FAVDADTLPA NARITHKSLF DNTLQGIELT DKPVSCFQGH PEASPGPQDV
GYLSDKFIGN MKAAKQA
