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Database: UniProt
Entry: X1JFF2_9ZZZZ
LinkDB: X1JFF2_9ZZZZ
Original site: X1JFF2_9ZZZZ 
ID   X1JFF2_9ZZZZ            Unreviewed;       214 AA.
AC   X1JFF2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
DE   Flags: Fragment;
GN   ORFNames=S03H2_64640 {ECO:0000313|EMBL:GAH80260.1};
OS   marine sediment metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=412755 {ECO:0000313|EMBL:GAH80260.1};
RN   [1] {ECO:0000313|EMBL:GAH80260.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAH80260.1};
RX   PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA   Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA   Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA   Takami H.;
RT   "High frequency of phylogenetically diverse reductive dehalogenase-
RT   homologous genes in deep subseafloor sedimentary metagenomes.";
RL   Front. Microbiol. 5:80-80(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC         phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC         ChEBI:CHEBI:456216; EC=6.3.4.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00043687};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAH80260.1}.
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DR   EMBL; BARU01042015; GAH80260.1; -; Genomic_DNA.
DR   AlphaFoldDB; X1JFF2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT   DOMAIN          10..134
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:GAH80260.1"
FT   NON_TER         214
FT                   /evidence="ECO:0000313|EMBL:GAH80260.1"
SQ   SEQUENCE   214 AA;  23917 MW;  AB8FDD93377419E0 CRC64;
     ASKAFSFTRQ ILVEESLKGW KEVEYEVVRD KYDNCITVCN MENFDPLGIH TGESIVVAPS
     QTLTNTEYHN LRELSIKVIR HIRIIGECNI QYALDPYSED YRVIEVNARL SRSSALASKA
     TGYPLAFIAA KLALGFGLHE LKNSVTKTTT ACFEPALDYI VCKIPRWDLN KFIGVSNLIG
     SSMKSVGEVM SIGRTFEEAI QKGLRMIGQG MHGF
//
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