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D3PQ55

- D3PQ55_MEIRD

UniProt

D3PQ55 - D3PQ55_MEIRD

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Protein

Carbamoyl-phosphate synthase large chain

Gene
carB, Mrub_0916, K649_04220
Organism
Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus ruber)
Status
Unreviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.UniRule annotationSAAS annotations

Cofactori

Binds 4 magnesium or manganese ions per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi286 – 2861Magnesium or manganese 1 By similarityUniRule annotation
Metal bindingi300 – 3001Magnesium or manganese 1 By similarityUniRule annotation
Metal bindingi300 – 3001Magnesium or manganese 2 By similarityUniRule annotation
Metal bindingi302 – 3021Magnesium or manganese 2 By similarityUniRule annotation
Metal bindingi843 – 8431Magnesium or manganese 3 By similarityUniRule annotation
Metal bindingi855 – 8551Magnesium or manganese 3 By similarityUniRule annotation
Metal bindingi855 – 8551Magnesium or manganese 4 By similarityUniRule annotation
Metal bindingi857 – 8571Magnesium or manganese 4 By similarityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi160 – 21758ATP By similarityUniRule annotationAdd
BLAST
Nucleotide bindingi718 – 77659ATP By similarityUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: UniProtKB-HAMAP
  3. magnesium ion binding Source: UniProtKB-HAMAP
  4. manganese ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  2. arginine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

LigaseUniRule annotationImported

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesisUniRule annotation, Pyrimidine biosynthesisUniRule annotation

Keywords - Ligandi

ATP-bindingUniRule annotation, MagnesiumUniRule annotation, ManganeseUniRule annotationSAAS annotations, Metal-bindingUniRule annotationSAAS annotations, Nucleotide-binding

Enzyme and pathway databases

BioCyciMRUB504728:GI6U-937-MONOMER.
UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase large chainUniRule annotation (EC:6.3.5.5UniRule annotation)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
Gene namesi
Name:carBUniRule annotationImported
Ordered Locus Names:Mrub_0916Imported
ORF Names:K649_04220Imported
OrganismiMeiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus ruber)Imported
Taxonomic identifieri504728 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeMeiothermus
ProteomesiUP000013026: Chromosome, UP000006655: Chromosome

Interactioni

Subunit structurei

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate By similarity.UniRule annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 329197ATP-grasp 1 By similarityUniRule annotationAdd
BLAST
Domaini692 – 884193ATP-grasp 2 By similarityUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 411411Carboxyphosphate synthetic domain By similarityUniRule annotationAdd
BLAST
Regioni412 – 554143Oligomerization domain By similarityUniRule annotationAdd
BLAST
Regioni555 – 950396Carbamoyl phosphate synthetic domain By similarityUniRule annotationAdd
BLAST
Regioni951 – 103888Allosteric domain By similarityUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the CarB family.UniRule annotation
Contains 2 ATP-grasp domains.UniRule annotation

Keywords - Domaini

RepeatUniRule annotation

Phylogenomic databases

HOGENOMiHOG000234582.
KOiK01955.
OMAiGSDRIWY.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.20. 2 hits.
HAMAPiMF_01210_B. CPSase_L_chain_B.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D3PQ55-1 [UniParc]FASTAAdd to Basket

« Hide

MPARTDLKKI MIIGSGPITI GQAAEFDYSG TQAVKALRSV GYQVVLVNSN     50
PATIMTDPEL AEGTYLEPLT VEFLEKIIAA ERPDALLPTL GGQTALNLSM 100
ALYEQGILEK YGVELIGANA AAIKKGEDRE EFQKAMLKIG VDVPRGKMVH 150
SLEEGLAFAR EVTGYPVVVR PSFTLGGTGG GIAENEAEFV EILSRGLSLS 200
PTHSALVEES IVGWKEYELE VMRDKNDTVV IITSIENLDP MGVHTGDSIT 250
VAPAQTLSDV EYQRMRDAAI AIIREIGVET GGSNIQFAID PKSGRMIVIE 300
MNPRVSRSSA LASKATGFPI AKIAALLAVG YTLDEIPNDI TQKTPASFEP 350
TIDYVVTKIP RFAFEKFSTL PNTNPGGFSD RLGTQMKSVG EVMAIGRTFK 400
ESFGKALRSL EADVRSEFSG LTTEELEARL YPSPTRIYAV LELLRRGVQV 450
DHLYEKTKIE PWFLTQLKEV VEAEHDLETE PHRLEDLEDW RYVKGLGLSD 500
ARVGELLGVS EAAARKQRLA AGCKPVYKTV DTCAAEFEAY TPYHYSTYEL 550
EDEVRPTSKP KVVILGSGPI RIGQGVEFDY ATVHAVWALR EAAIPPERPG 600
EAGARGYETI MVNSNPETVS TDYDTADRLY FEPLTLEDVL NLAEHEKPIG 650
VIATLGGQTP LKLAKKLAEA GVPLLGTSWE AIHKAEDRAE FNQLCAALGI 700
PQPKGAVART PEEALKLAET LGYPLMARPS YVLGGRAMQV VRNPEELRWY 750
LSGIYAALAE RPSILLDQYL ENALELDVDA LCDGKQVVVA GIMEHIERAG 800
VHSGDSATIL PPISLTPEQL ETVKAYTRKL ALAVGVRGLI NVQYAIKDGV 850
VYILEANPRA SRTVPFVSKA IGHPLAKYAA LIAVGHTLEE LGFTQDPTPS 900
FYAVKEVLIP WLKFPGVIPV LGPEMRSTGE SMGIDTDPYL AYYRAELGVG 950
QRLPLSGKVR FIGAEQLKPD WEAAGFEVSE GDYDLLIALT PDPELRRAVE 1000
TGKPFITTLE GARWSLEAIL RARHSNLPVR SLQAWHGR 1038
Length:1,038
Mass (Da):113,358
Last modified:April 20, 2010 - v1
Checksum:iA3DA9A98A1E25318
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001743 Genomic DNA. Translation: ADD27681.1.
CP005385 Genomic DNA. Translation: AGK04146.1.
RefSeqiWP_013013200.1. NC_021081.1.
YP_003506701.1. NC_013946.1.
YP_007879643.1. NC_021081.1.

Genome annotation databases

EnsemblBacteriaiADD27681; ADD27681; Mrub_0916.
AGK04146; AGK04146; K649_04220.
GeneIDi15335456.
8879003.
KEGGimrb:Mrub_0916.
mre:K649_04220.
PATRICi35357964. VBIMeiRub128672_0920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001743 Genomic DNA. Translation: ADD27681.1 .
CP005385 Genomic DNA. Translation: AGK04146.1 .
RefSeqi WP_013013200.1. NC_021081.1.
YP_003506701.1. NC_013946.1.
YP_007879643.1. NC_021081.1.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADD27681 ; ADD27681 ; Mrub_0916 .
AGK04146 ; AGK04146 ; K649_04220 .
GeneIDi 15335456.
8879003.
KEGGi mrb:Mrub_0916.
mre:K649_04220.
PATRICi 35357964. VBIMeiRub128672_0920.

Phylogenomic databases

HOGENOMi HOG000234582.
KOi K01955.
OMAi GSDRIWY.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00171 .
UPA00070 ; UER00115 .
BioCyci MRUB504728:GI6U-937-MONOMER.

Family and domain databases

Gene3Di 1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.20. 2 hits.
HAMAPi MF_01210_B. CPSase_L_chain_B.
InterProi IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view ]
Pfami PF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
[Graphical view ]
PRINTSi PR00098. CPSASE.
SMARTi SM01096. CPSase_L_D3. 1 hit.
[Graphical view ]
SUPFAMi SSF48108. SSF48108. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsi TIGR01369. CPSaseII_lrg. 1 hit.
PROSITEi PS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35948 / DSM 1279 / VKM B-1258 / 21.
  2. "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT Sequencing Data."
    Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J., Eichler E., Turner S.W.
    Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM 1279Imported.
  3. Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.
    Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: DSM 1279Imported.

Entry informationi

Entry nameiD3PQ55_MEIRD
AccessioniPrimary (citable) accession number: D3PQ55
Entry historyi
Integrated into UniProtKB/TrEMBL: April 20, 2010
Last sequence update: April 20, 2010
Last modified: September 3, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi