CARA_ZYMMO
ID CARA_ZYMMO Reviewed; 374 AA.
AC O50235; Q5NM18;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 25-MAY-2022, entry version 128.
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}; OrderedLocusNames=ZMO1618;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee J.S., Jin S.J., Kang H.L., Kang H.S.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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 {ECO:0000255|HAMAP-Rule:MF_01209}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000255|HAMAP-
CC Rule:MF_01209}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC70355.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAV90242.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF086791; AAC70355.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE008692; AAV90242.1; ALT_INIT; Genomic_DNA.
DR PIR; T33716; T33716.
DR AlphaFoldDB; O50235; -.
DR SMR; O50235; -.
DR STRING; 264203.ZMO1618; -.
DR MEROPS; C26.954; -.
DR PRIDE; O50235; -.
DR EnsemblBacteria; AAV90242; AAV90242; ZMO1618.
DR KEGG; zmo:ZMO1618; -.
DR eggNOG; COG0505; Bacteria.
DR HOGENOM; CLU_035901_2_1_5; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001173; Chromosome.
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; Reference proteome.
FT CHAIN 1..374
FT /note="Carbamoyl-phosphate synthase small chain"
FT /id="PRO_0000112354"
FT DOMAIN 187..374
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT REGION 1..183
FT /note="CPSase"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT ACT_SITE 348
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
FT ACT_SITE 350
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01209"
SQ SEQUENCE 374 AA; 40808 MW; 4C6BFA63818FE09E CRC64;
MVLADGQMIW GRGFGATGAK VGEVCFHTAM TGYEEIMTDP SFASQIINFT FPHIGNVGAN
REDVEAKTLH ALGCIVREDV TAPSNFRSLW RFDSWLKDHD RIGLAGVDTR ALTGLLRKKG
AQNAVIAHDP KGQFDIPALI ETARSWAGLQ GMDLARSVST HQSYNWQEGI WSLQNGYSVV
DNQKGPHVVA IDYGLKHNIL RNLVEAGARV TVVKATASFD EVMAHKPDGV FLSNGPGDPA
ATAEYAVPVI RQLLDIKMPI FGICLGHQLL ALAVGATTYK MHQGHRGANH PVKRLDDSKV
EITSMNHGFA VATDSLPEQA RPTHLSLFDG SLAGLELTDR PAFSVQYHPE ASPGPQDSYY
LFTKFIDLIA KERP
