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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
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.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 4 Mg2+ or Mn2+ ions per subunit.By similarity

Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes carbamoyl phosphate from bicarbonate.
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamoyl-phosphate synthase large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes carbamoyl phosphate from bicarbonate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

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 large chain (carB), Carbamoyl-phosphate synthase small chain (carA)
  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 bindingi283Magnesium or manganese 1By similarity1
Metal bindingi297Magnesium or manganese 1By similarity1
Metal bindingi297Magnesium or manganese 2By similarity1
Metal bindingi299Magnesium or manganese 2By similarity1
Metal bindingi814Magnesium or manganese 3By similarity1
Metal bindingi829Magnesium or manganese 3By similarity1
Metal bindingi829Magnesium or manganese 4By similarity1
Metal bindingi831Magnesium or manganese 4By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi157 – 214ATPBy similarityAdd BLAST58
Nucleotide bindingi690 – 747ATPBy similarityAdd BLAST58

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis

Keywords - Ligandi

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

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase large chain (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
Gene namesi
Name:carB
Ordered Locus Names:MTH_996/MTH_997
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001450801 – 1060Carbamoyl-phosphate synthase large chainAdd BLAST1060

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

STRINGi187420.MTH996.

Structurei

3D structure databases

ProteinModelPortaliO27077.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini131 – 326ATP-grasp 1Add BLAST196
Domaini664 – 858ATP-grasp 2Add BLAST195

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 400Carboxyphosphate synthetic domainAdd BLAST400
Regioni401 – 539Oligomerization domainAdd BLAST139
Regioni540 – 926Carbamoyl phosphate synthetic domainAdd BLAST387
Regioni927 – 1060Allosteric domainAdd BLAST134

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiarCOG01594. Archaea.
COG0458. LUCA.
KOiK01955.

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.

O27077-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRDESINKV LIIGSGPIQI GQAAEFDYSG SQACKSLREE GIETVLVNSN
60 70 80 90 100
PATIQTDMEM ADRVYVEPLT PEIVAKIIQK EKPDAVLPTM GGQTGLNVAT
110 120 130 140 150
GLAEMGALEG VRVIGSSIET IRNVEDRDLF DSFMKKLNEP VPAARAVSSV
160 170 180 190 200
EEALEAVEEI GYPVIVRPAF TLGGTGGGVA HSRDELIEIA TRGLEMSFIN
210 220 230 240 250
QVLIDQSVLG WKEFEYEVMR DRNDTCIIVL CNMENIDPMG IHTGESVVVA
260 270 280 290 300
PAQTLSDEDN QRLRDAAIKI IRALKIEGGC NIQFAVHPET GEYKVIEVNP
310 320 330 340 350
RVSRSSALAS KATGYPIAKI AAKIAVGMTL DEIQNDITKE TPASFEPTID
360 370 380 390 400
YVVTKIPRWP FDKFKGISRE IGVQMKSTGE VMAIGRTLEE SLNKAIRSLD
410 420 430 440 450
IGADGFTETP YTRADLENPT DQRLFQVYTA LRDGMSIEEI HGLTQIDPFF
460 470 480 490 500
LQKISNIAEF ESSITRESLE DPRILLKAKR MGFSDSRLAS LTGMDESSIR
510 520 530 540 550
ALRLENNIKP VYKMVDTCAA EFEARTPYYY GCYDLEDEVE VSDRRKVLII
560 570 580 590 600
GSGPIRIGQG IEFDYCCVHA AMALTEDGYE TIMVNNNPET VSTDYDISDK
610 620 630 640 650
LYFEPLTLED VLAIIEKEKP EGVVVQFGGQ TSINLAVPLA EAGVRILGTP
660 670 680 690 700
HESIDRVEDR ERFTEVLNKL GIPQAPYGIA KSFEDARAVA ERIGYPVLVR
710 720 730 740 750
PSYVLGGRAM EIVYDDVELE EYMREAVRVS PEHPILVDKF LEDAIEVDVD
760 770 780 790 800
ALCDGTDVYI GGIMEHIEEA GVHSGDSACV IPPQSIPEDI IDTIKEYTRK
810 820 830 840 850
LALELEVVGL INIQYAVKPD SDPSVYILEA NPRASRTVPF VSKATGVPLA
860 870 880 890 900
KMAARLMMGA KLRDLGLTEE KDIEHVAVKE SVFPFIKLPG ADSVLGPEMK
910 920 930 940 950
STGEAMGIDE NFGIAYYKSQ LSASMDLLNE GKVFISVRDQ DKDKIADIVK
960 970 980 990 1000
KADELGFRIM ATRGTARAVS DIADIEVVRK VSQGSPNIRD AILDGEVGLI
1010 1020 1030 1040 1050
INTPSGKQSA DDGYLIRRMA VELGIPYVTT LAGARAALNA IEAVRMGKIT
1060
VKSLDEYHGM
Length:1,060
Mass (Da):116,278
Last modified:August 2, 2002 - v2
Checksum:i56716027BA1EDDCA
GO

Sequence cautioni

The sequence AAB85494 differs from that shown. Reason: Frameshift at position 230. Produces two separate ORFs.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85493.1. Frameshift.
AE000666 Genomic DNA. Translation: AAB85494.1. Frameshift.
PIRiD69233.
E69233.

Genome annotation databases

EnsemblBacteriaiAAB85493; AAB85493; MTH_996.
AAB85494; AAB85494; MTH_997.
KEGGimth:MTH_996.
mth:MTH_997.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB85493.1. Frameshift.
AE000666 Genomic DNA. Translation: AAB85494.1. Frameshift.
PIRiD69233.
E69233.

3D structure databases

ProteinModelPortaliO27077.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH996.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB85493; AAB85493; MTH_996.
AAB85494; AAB85494; MTH_997.
KEGGimth:MTH_996.
mth:MTH_997.

Phylogenomic databases

eggNOGiarCOG01594. Archaea.
COG0458. LUCA.
KOiK01955.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

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_METTH
AccessioniPrimary (citable) accession number: O27077
Secondary accession number(s): O27078
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: August 2, 2002
Last modified: November 30, 2016
This is version 115 of the entry and version 2 of the sequence. [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

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.