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Protein

Carbamoyl-phosphate synthase pyrimidine-specific large chain

Gene

pyrAB

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Catalytic activityi

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

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.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase pyrimidine-specific small chain (pyrAA), Carbamoyl-phosphate synthase pyrimidine-specific large chain (pyrAB)
  2. Aspartate carbamoyltransferase (pyrB)
  3. 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 1By similarity1
Metal bindingi298Magnesium or manganese 1By similarity1
Metal bindingi298Magnesium or manganese 2By similarity1
Metal bindingi300Magnesium or manganese 2By similarity1
Metal bindingi820Magnesium or manganese 3By similarity1
Metal bindingi832Magnesium or manganese 3By similarity1
Metal bindingi832Magnesium or manganese 4By similarity1
Metal bindingi834Magnesium or manganese 4By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPBy similarityAdd BLAST58
Nucleotide bindingi697 – 754ATPBy similarityAdd BLAST58

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processPyrimidine biosynthesis
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBHAL272558:G1G3A-2608-MONOMER
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
Ordered Locus Names:BH2536
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001258 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001449871 – 1062Carbamoyl-phosphate synthase pyrimidine-specific large chainAdd BLAST1062

Proteomic databases

PRIDEiQ9K9V9

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

Protein-protein interaction databases

STRINGi272558.BH2536

Structurei

3D structure databases

ProteinModelPortaliQ9K9V9
SMRiQ9K9V9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 327ATP-grasp 1Add BLAST195
Domaini671 – 861ATP-grasp 2Add BLAST191
Domaini930 – 1062MGS-likePROSITE-ProRule annotationAdd BLAST133

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 401Carboxyphosphate synthetic domainAdd BLAST401
Regioni402 – 546Oligomerization domainAdd BLAST145
Regioni547 – 929Carbamoyl phosphate synthetic domainAdd BLAST383
Regioni930 – 1062Allosteric domainAdd BLAST133

Sequence similaritiesi

Belongs to the CarB family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CU6 Bacteria
COG0458 LUCA
HOGENOMiHOG000234583
KOiK01955
OMAiAVFPFNK
OrthoDBiPOG091H01IP

Family and domain databases

CDDicd01424 MGS_CPS_II, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.40.50.1380, 1 hit
HAMAPiMF_01210_A CPSase_L_chain_A, 1 hit
MF_01210_B CPSase_L_chain_B, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
IPR006275 CarbamoylP_synth_lsu
IPR005480 CarbamoylP_synth_lsu_oligo
IPR036897 CarbamoylP_synth_lsu_oligo_sf
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR005483 CbamoylP_synth_lsu_CPSase_dom
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR033937 MGS_CPS_CarB
IPR016185 PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF02786 CPSase_L_D2, 2 hits
PF02787 CPSase_L_D3, 1 hit
PF02142 MGS, 1 hit
PRINTSiPR00098 CPSASE
SMARTiView protein in SMART
SM01096 CPSase_L_D3, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF48108 SSF48108, 1 hit
SSF52335 SSF52335, 1 hit
SSF52440 SSF52440, 2 hits
TIGRFAMsiTIGR01369 CPSaseII_lrg, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 2 hits
PS00866 CPSASE_1, 2 hits
PS00867 CPSASE_2, 2 hits
PS51855 MGS, 1 hit

Sequencei

Sequence statusi: Complete.

Q9K9V9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKREDIKKI LVIGSGPIVI GQAAEFDYAG TQACQALKEE GYEVILVNSN
60 70 80 90 100
PATIMTDTTM ADRVYIEPLT LEFVSRIIRM ERPDGILPTL GGQTGLNMAV
110 120 130 140 150
ELDQAGILKE YNVELLGTKL DSIQQAEDRD LFRALMKELN EPVPDSEIIH
160 170 180 190 200
TLEEAYTFVE RVGYPIIVRP AYTLGGTGGG LVYNEEDLVE IVTSGLKYSP
210 220 230 240 250
VTQCLVEKSI AGFKEIEYEV MRDGKDHAIV VCNMENIDPV GVHTGDSIVV
260 270 280 290 300
APSQTLSDRE YQMLRNSSLK IIRALGIEGG CNVQFALDPD SFQYYIIEVN
310 320 330 340 350
PRVSRSSALA SKATGYPIAK IAAKIAVGYT LDELLNPITQ TTYASFEPAL
360 370 380 390 400
DYVVSKIPRW PFDKFEAANR SLGTQMKATG EVMAIGRNLE ESLLKAVRSL
410 420 430 440 450
EAGVYHLDQP DVNDLDKESL EKKLTKPDDE RLFALGEAIR RGYTIEELWA
460 470 480 490 500
LTKIDRFFLR SFARIIQLET QLKENVGDLE LLKEAKERGF SDMIIADLWG
510 520 530 540 550
TSEQEVYELR MNHGLSPVYK MVDTCAAEFA SATPYFYGTY EEENESERTD
560 570 580 590 600
KKSILVLGSG PIRIGQGIEF DYATVHTVWA IKEAGYEAII VNNNPETVST
610 620 630 640 650
DFSTSDKLYF EPLTVEDVMH IVNLEQPEGV IVQFGGQTAI NLASELAARG
660 670 680 690 700
VKIIGTALED MDRAEDRDKF EQTLVELNIP QPLGDTATSI EEARQIAERI
710 720 730 740 750
GYPVLVRPSY VLGGRAMEIV YKEEELLNYM AHAVKVNPKH PVLIDRYLTG
760 770 780 790 800
KELEVDAISD GENVYIPGIM EHIERAGVHS GDSIAVYPPQ TVPESLKQKL
810 820 830 840 850
IERTIELARG LRIVGLLNIQ FVWHKDDVYV LEVNPRSSRT VPFLSKVTGV
860 870 880 890 900
PMANVATKVM LGKTLPQLGY ETGYHPEAKE VSVKVPVFSF AKLRRVDITL
910 920 930 940 950
GPEMKSTGEV MGRDKTLEKA LYKGLIASGM SIPTHGSVLF TIADKDKQEA
960 970 980 990 1000
ISLAKRFYQI GFSILATEGT AHILHEEGIP VTTVNKISDE KPHLLDVIRA
1010 1020 1030 1040 1050
GDAQFVINTL TRGKQPARDG FRIRRESVEN GVVCLTSLDT AEALLRVLES
1060
ITFSAESMPV MQ
Length:1,062
Mass (Da):117,814
Last modified:October 1, 2000 - v1
Checksum:i533DD62812EAA691
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA Translation: BAB06255.1
PIRiH83966
RefSeqiWP_010898687.1, NC_002570.2

Genome annotation databases

EnsemblBacteriaiBAB06255; BAB06255; BAB06255
KEGGibha:BH2536

Similar proteinsi

Entry informationi

Entry nameiCARB_BACHD
AccessioniPrimary (citable) accession number: Q9K9V9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: October 1, 2000
Last modified: March 28, 2018
This is version 121 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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