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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 Mg2+ or Mn2+ ions per subunit.By similarity

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB_1), Carbamoyl-phosphate synthase (glutamine-hydrolyzing) (B4109_0960), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase pyrimidine-specific large chain (pyrAB), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase (glutamine-hydrolyzing) (B4114_0995), Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA_1), Carbamoyl-phosphate synthase (glutamine-hydrolyzing) (carB_2), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase (glutamine-hydrolyzing) (AA904_03185), Carbamoyl-phosphate synthase large chain (carB)
  2. Aspartate carbamoyltransferase (pyrB), Aspartate carbamoyltransferase (pyrB), Aspartate carbamoyltransferase (pyrB), Aspartate carbamoyltransferase (pyrB)
  3. Dihydroorotase (pyrC), Dihydroorotase (pyrC), Dihydroorotase (pyrC), Dihydroorotase (pyrC), Dihydroorotase (pyrC)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi284Magnesium or manganese 1UniRule annotation1
Metal bindingi298Magnesium or manganese 1UniRule annotation1
Metal bindingi298Magnesium or manganese 2UniRule annotation1
Metal bindingi300Magnesium or manganese 2UniRule annotation1
Metal bindingi820Magnesium or manganese 3UniRule annotation1
Metal bindingi832Magnesium or manganese 3UniRule annotation1
Metal bindingi832Magnesium or manganese 4UniRule annotation1
Metal bindingi834Magnesium or manganese 4UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPUniRule annotationAdd BLAST58
Nucleotide bindingi697 – 754ATPUniRule annotationAdd BLAST58

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001449891 – 1064Carbamoyl-phosphate synthase pyrimidine-specific large chainAdd BLAST1064

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)DescriptionActionsGraphical viewLength
Domaini133 – 327ATP-grasp 1UniRule annotationAdd BLAST195
Domaini671 – 861ATP-grasp 2UniRule annotationAdd BLAST191

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 401Carboxyphosphate synthetic domainAdd BLAST401
Regioni402 – 546Oligomerization domainAdd BLAST145
Regioni547 – 929Carbamoyl phosphate synthetic domainAdd BLAST383
Regioni930 – 1064Allosteric domainAdd BLAST135

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Family and domain databases

CDDicd01424. MGS_CPS_II. 1 hit.
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. 1 hit.
MF_01210_B. CPSase_L_chain_B. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR011607. MGS-like_dom.
IPR033937. MGS_CPS_CarB.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02786. 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

CDDicd01424. MGS_CPS_II. 1 hit.
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. 1 hit.
MF_01210_B. CPSase_L_chain_B. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR011607. MGS-like_dom.
IPR033937. MGS_CPS_CarB.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02786. 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...

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: November 30, 2016
This is version 89 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

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 one 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.