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Protein

Carbamoyl-phosphate synthase pyrimidine-specific large chain

Gene

pyrAB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: 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 annotation

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 4 Mg(2+) or Mn2+ ions per subunit.By similarity

Pathwayi

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 21658ATPUniRule annotationAdd
BLAST
Nucleotide bindingi697 – 75458ATPUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
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

BRENDAi6.3.5.5. 623.
UniPathwayiUPA00070; UER00115.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase pyrimidine-specific large chain (EC:6.3.5.5UniRule annotation)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chainUniRule annotation
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 chainPRO_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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

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

« Hide

        10         20         30         40         50
MPKRRDIETI LVIGSGPIVI GQAAEFDYAG TQACLALKEE GYKVILVNSN
60 70 80 90 100
PATIMTDTEI ADKVYMEPLT LDFVARIIRK ERPDAILPTL GGQTGLNLAV
110 120 130 140 150
ELAKAGVLEE CGVEILGTKL EAIEKAEDRE QFRALMNELG EPVPESAIIH
160 170 180 190 200
SLEEAYAFVE QIGYPVIVRP AFTLGGTGGG ICTNEEELVE IVSTGLKLSP
210 220 230 240 250
VHQCLLERSI AGYNQIEYEV MRDANDNAIV VCNMENIDPV GIHTGDSIVV
260 270 280 290 300
APSQTLSDRE YQLLRNASLK IIRALGIEGG CNVQLALDPD SFRYYVIEVN
310 320 330 340 350
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEMINPVTG KTYACFEPAL
360 370 380 390 400
DYVVTKIPRF PFDKFESANR RLGTQMKATG EVMSIGRTFE ESLLKAVRSL
410 420 430 440 450
EIGVHHLELN EAKTAADDVM EKRIRKAGDE RLFYIAEALR RGVTVETLHE
460 470 480 490 500
WSQIDRFFLH KIQNIIEMET VLKNHPGDLD VLKKAKGLGF SDAAIAALWN
510 520 530 540 550
KTERDVYALR RQEGIVPVYK MVDTCAAEFT SETPYYYSTY EEENESIVTE
560 570 580 590 600
KPSVIVLGSG PIRIGQGIEF DYATVHCVLA IKQAGYEAII INNNPETVST
610 620 630 640 650
DFSTSDKLYF EPLTAEDVMH VIDLEQPVGV IVQFGGQTAI NLAAELEARG
660 670 680 690 700
VRLLGTTLED LDRAEDRDKF EQALSELGIP KPAGKTAVSV EEAVAIAEEI
710 720 730 740 750
GYPVLVRPSY VLGGRAMEIV YNREELLHYM EHAVRVNPQH PVLVDRYITG
760 770 780 790 800
KEVEVDAIAD GETVVIPGIM EHIERAGVHS GDSIAVYPPQ TLSDDVIAKI
810 820 830 840 850
TDYTVKLARG LHIVGLLNIQ FVVAGSDVYV LEVNPRSSRT VPFLSKITGV
860 870 880 890 900
PMANLATKAI LGAKLADMGY ETGVCPVRPG VYVKVPVFSF AKLRNVDISL
910 920 930 940 950
GPEMKSTGEV IGKDVTFEKA LYKGLVASGI QIQPHGAVLL TVADKDKEEA
960 970 980 990 1000
VELARRFADI GYQLLATNGT AETLKAAGIP VTVVNKIHSA SPNILDVIRQ
1010 1020 1030 1040 1050
GKAQVVINTL TKGKQPESDG FRIRREVENG IPCLTSLDTA RAMLQVLESM
1060
TFSTTAMTEG LVRS
Length:1,064
Mass (Da):116,243
Last modified:June 1, 1998 - v1
Checksum:iF5AD61003AA3FC4B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001805 Genomic DNA. Translation: CAA05020.1.
PIRiT44419.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001805 Genomic DNA. Translation: CAA05020.1.
PIRiT44419.

3D structure databases

ProteinModelPortaliO50302.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00070; UER00115.
BRENDAi6.3.5.5. 623.

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]
ProtoNetiSearch...

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(1997) [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: April 1, 2015
This is version 87 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.