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O50302

- CARB_GEOSE

UniProt

O50302 - CARB_GEOSE

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Protein

Carbamoyl-phosphate synthase pyrimidine-specific large chain

Gene
pyrAB
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Binds 4 magnesium or manganese ions per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi284 – 2841Magnesium or manganese 1 By similarity
Metal bindingi298 – 2981Magnesium or manganese 1 By similarity
Metal bindingi298 – 2981Magnesium or manganese 2 By similarity
Metal bindingi300 – 3001Magnesium or manganese 2 By similarity
Metal bindingi820 – 8201Magnesium or manganese 3 By similarity
Metal bindingi832 – 8321Magnesium or manganese 3 By similarity
Metal bindingi832 – 8321Magnesium or manganese 4 By similarity
Metal bindingi834 – 8341Magnesium or manganese 4 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 21658ATP By similarityAdd
BLAST
Nucleotide bindingi697 – 75458ATP By similarityAdd
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

Ligase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00070; UER00115.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase pyrimidine-specific large chain (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
Gene namesi
Name:pyrAB
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10641064Carbamoyl-phosphate synthase pyrimidine-specific large chainUniRule annotationPRO_0000144989Add
BLAST

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.

Structurei

3D structure databases

ProteinModelPortaliO50302.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 327195ATP-grasp 1Add
BLAST
Domaini671 – 861191ATP-grasp 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 401401Carboxyphosphate synthetic domainUniRule annotationAdd
BLAST
Regioni402 – 546145Oligomerization domainUniRule annotationAdd
BLAST
Regioni547 – 929383Carbamoyl phosphate synthetic domainUniRule annotationAdd
BLAST
Regioni930 – 1064135Allosteric domainUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
HAMAPiMF_01210_A. CPSase_L_chain_A.
MF_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.
IPR011607. MGS-like_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.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O50302-1 [UniParc]FASTAAdd to Basket

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MPKRRDIETI LVIGSGPIVI GQAAEFDYAG TQACLALKEE GYKVILVNSN     50
PATIMTDTEI ADKVYMEPLT LDFVARIIRK ERPDAILPTL GGQTGLNLAV 100
ELAKAGVLEE CGVEILGTKL EAIEKAEDRE QFRALMNELG EPVPESAIIH 150
SLEEAYAFVE QIGYPVIVRP AFTLGGTGGG ICTNEEELVE IVSTGLKLSP 200
VHQCLLERSI AGYNQIEYEV MRDANDNAIV VCNMENIDPV GIHTGDSIVV 250
APSQTLSDRE YQLLRNASLK IIRALGIEGG CNVQLALDPD SFRYYVIEVN 300
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEMINPVTG KTYACFEPAL 350
DYVVTKIPRF PFDKFESANR RLGTQMKATG EVMSIGRTFE ESLLKAVRSL 400
EIGVHHLELN EAKTAADDVM EKRIRKAGDE RLFYIAEALR RGVTVETLHE 450
WSQIDRFFLH KIQNIIEMET VLKNHPGDLD VLKKAKGLGF SDAAIAALWN 500
KTERDVYALR RQEGIVPVYK MVDTCAAEFT SETPYYYSTY EEENESIVTE 550
KPSVIVLGSG PIRIGQGIEF DYATVHCVLA IKQAGYEAII INNNPETVST 600
DFSTSDKLYF EPLTAEDVMH VIDLEQPVGV IVQFGGQTAI NLAAELEARG 650
VRLLGTTLED LDRAEDRDKF EQALSELGIP KPAGKTAVSV EEAVAIAEEI 700
GYPVLVRPSY VLGGRAMEIV YNREELLHYM EHAVRVNPQH PVLVDRYITG 750
KEVEVDAIAD GETVVIPGIM EHIERAGVHS GDSIAVYPPQ TLSDDVIAKI 800
TDYTVKLARG LHIVGLLNIQ FVVAGSDVYV LEVNPRSSRT VPFLSKITGV 850
PMANLATKAI LGAKLADMGY ETGVCPVRPG VYVKVPVFSF AKLRNVDISL 900
GPEMKSTGEV IGKDVTFEKA LYKGLVASGI QIQPHGAVLL TVADKDKEEA 950
VELARRFADI GYQLLATNGT AETLKAAGIP VTVVNKIHSA SPNILDVIRQ 1000
GKAQVVINTL TKGKQPESDG FRIRREVENG IPCLTSLDTA RAMLQVLESM 1050
TFSTTAMTEG LVRS 1064
Length:1,064
Mass (Da):116,243
Last modified:June 1, 1998 - v1
Checksum:iF5AD61003AA3FC4B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ001805 Genomic DNA. Translation: CAA05020.1.
PIRiT44419.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ001805 Genomic DNA. Translation: CAA05020.1 .
PIRi T44419.

3D structure databases

ProteinModelPortali O50302.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00070 ; UER00115 .

Family and domain databases

Gene3Di 1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
HAMAPi MF_01210_A. CPSase_L_chain_A.
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.
IPR011607. MGS-like_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.
PF02142. MGS. 1 hit.
[Graphical view ]
PRINTSi PR00098. CPSASE.
SMARTi SM01096. CPSase_L_D3. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48108. SSF48108. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsi TIGR01369. CPSaseII_lrg. 1 hit.
PROSITEi PS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The pyrAb gene coding for the large subunit of carbamoylphosphate synthetase from Bacillus stearothermophilus: molecular cloning and functional characterization."
    Vlaskova H., Krasny L., Fucik V., Jonak J.
    Folia Biol. (Praha) 44:163-172(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CCM 2184.

Entry informationi

Entry nameiCARB_GEOSE
AccessioniPrimary (citable) accession number: O50302
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: June 1, 1998
Last modified: February 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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