ID A0A2Z2HJ76_9ARCH Unreviewed; 340 AA.
AC A0A2Z2HJ76;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012738};
DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
GN Name=guaAA_3 {ECO:0000313|EMBL:ARS64157.1};
GN ORFNames=NMSP_0536 {ECO:0000313|EMBL:ARS64157.1};
OS Candidatus Nitrosomarinus catalina.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosomarinus.
OX NCBI_TaxID=1898749 {ECO:0000313|EMBL:ARS64157.1, ECO:0000313|Proteomes:UP000249949};
RN [1] {ECO:0000313|EMBL:ARS64157.1, ECO:0000313|Proteomes:UP000249949}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPOT01 {ECO:0000313|EMBL:ARS64157.1,
RC ECO:0000313|Proteomes:UP000249949};
RX PubMed=28418097;
RA Ahlgren N.A., Chen Y., Needham D.M., Parada A.E., Sachdeva R., Trinh V.,
RA Chen T., Fuhrman J.A.;
RT "Genome and epigenome of a novel marine Thaumarchaeota strain suggest viral
RT infection, phosphorothioation DNA modification and multiple restriction
RT systems.";
RL Environ. Microbiol. 19:2434-2452(2017).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SIMILARITY: Belongs to the CarA family.
CC {ECO:0000256|ARBA:ARBA00007800}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; CP021324; ARS64157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z2HJ76; -.
DR KEGG; nct:NMSP_0536; -.
DR Proteomes; UP000249949; Chromosome.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 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 NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 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 SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ARS64157.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 1..108
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
FT ACT_SITE 228
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 313
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 340 AA; 37776 MW; E3B110A8D29527E1 CRC64;
MVGYTEALTD PSYNGQLLTL TYPLVGNYGI PDPKITDEDG ISKYFESDKI QIRGLVIHEL
SLTASHWNLS MTLDEWMYNE KVPGISGIDT RALTMKLRNS GVMMGALVVS DSEIDVEEVK
KQLASATHYD SEQFMDEVST KQEKIYGSEE QTVVIVDTGA KNAIIRNVRE IGYRAILVPW
NTPYEKIMSY NPKGVVLSSG PGDPQKCPDT ISAVKKLIEN NVPTLGICLG AQIIGIAGNT
DTYKLKYGHR GQNKPCINLD NNQVYVTSQN HGYGITPESL EKSDFDLWFK NADDKTVEGI
KHKKQNCIAV QFHPEAAPGP NDCKFIFEKL KTLMESKTNA
//
