ID B1YJM4_EXIS2 Unreviewed; 1010 AA.
AC B1YJM4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:ACB60054.1};
GN OrderedLocusNames=Exig_0573 {ECO:0000313|EMBL:ACB60054.1};
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543 {ECO:0000313|EMBL:ACB60054.1, ECO:0000313|Proteomes:UP000001681};
RN [1] {ECO:0000313|EMBL:ACB60054.1, ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RX PubMed=16489412; DOI=10.1007/s00792-005-0497-5;
RA Rodrigues D.F., Goris J., Vishnivetskaya T., Gilichinsky D.,
RA Thomashow M.F., Tiedje J.M.;
RT "Characterization of Exiguobacterium isolates from the Siberian permafrost.
RT Description of Exiguobacterium sibiricum sp. nov.";
RL Extremophiles 10:285-294(2006).
RN [2] {ECO:0000313|EMBL:ACB60054.1, ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RX PubMed=19019206; DOI=10.1186/1471-2164-9-547;
RA Rodrigues D.F., Ivanova N., He Z., Huebner M., Zhou J., Tiedje J.M.;
RT "Architecture of thermal adaptation in an Exiguobacterium sibiricum strain
RT isolated from 3 million year old permafrost: a genome and transcriptome
RT approach.";
RL BMC Genomics 9:547-547(2008).
RN [3] {ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; CP001022; ACB60054.1; -; Genomic_DNA.
DR RefSeq; WP_012369478.1; NC_010556.1.
DR AlphaFoldDB; B1YJM4; -.
DR STRING; 262543.Exig_0573; -.
DR KEGG; esi:Exig_0573; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_9; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000001681; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000001681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 130..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 667..852
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 1010 AA; 111453 MW; 2C1D3F1AD79A4704 CRC64;
MQEVKKVLVI GSGPIVIGQA AEFDYSGTQA CQTLREAGCE VMLMNSNPAT IMTDPSTADH
IYIEAMTLEK ATAIIKRERP THLLATVGGQ TALNLALSLE EAGVLDQYQV KLLGTSLETI
RDGEDRERFK QRMLELDQPL PISQTIETLE ELEGFMEKAG VPLVVRPAFT LGGTGGGIAQ
TKEEARKLAA NGLQASPISQ CLVEASIAGY KEVEYEVMRD AFDTTIIVCN MENIDPVGVH
TGDSVVFAPI QSISDKMNQI LRTASREIVS ALGVVGGCNI QFAIHPTEQT YYVIEVNPRV
SRSSALASKA TGYPIAKLAT RLALGERLDD CINPVTKETM ASFEPVLDYV TAKVPCFPFD
LFPGSDRSLG TQMKATGESM AMGKTLEEAL QKAWRGAGIE QAPLYPNWMK QADTEVLWQE
VNQITDRRLL AMLALLDRKA ATHEELAEKT QIQSLFLTTL ETLILMQESL DLESKESLQQ
AKGFGFTDQQ IAQITDVPLE VVQQQRNTFL IQPSFQMIDT CGAEFSSLTP YFYGSWSGRT
EVTPSSRKKV AVLGAGPIRI GQGIEFDYCS VHAVRALQKA GYETIMINNN PETVSTDFEV
ADRLYVEPLT IEDVVHVLEA EQCRQVLVQF GGQTAITLAA ELEELGYQLL GTTADTIDEM
EDRDRFYQFL DRLQIDRILG QEVSNEEELT AIVKELGYPL MIRPSYVIGG KGMHRLTTAT
DLEKLLPEMV FPILVDAYIE GHEFEVDCIS DKTTTYVPVI MEQIEAAGVH SGDSTMILPP
VSALASLQDE IEQIAQTIGQ HLDYQGAFNI QFVVKDQTVY VLEINPRASR TLPIVSKVTG
QPLLEWAVQA AIGMKVEALP ANRLTLPFHA VKTPVFSTLK LRGVDPMTGP VMRSTGETLQ
WTEAGLAKER FVFDQTTKTA MAKRTLRICG AGTDAWSEGA AVQPDTEFDT CLVFFSKSES
EREQREKALA QGAIVITEEH LAQYFESVQT IPMCTVKPLS EWTTQKERIQ
//
