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Protein

Carbamoyl-phosphate synthase large chain

Gene

carB

Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
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: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes carbamoyl phosphate from bicarbonate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB)
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.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase small chain (carA), Carbamoyl-phosphate synthase large chain (carB)
  2. Aspartate carbamoyltransferase (pyrB)
  3. Dihydroorotase (ZMO1689)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi287 – 2871Magnesium or manganese 1UniRule annotation
Metal bindingi301 – 3011Magnesium or manganese 1UniRule annotation
Metal bindingi301 – 3011Magnesium or manganese 2UniRule annotation
Metal bindingi303 – 3031Magnesium or manganese 2UniRule annotation
Metal bindingi866 – 8661Magnesium or manganese 3UniRule annotation
Metal bindingi878 – 8781Magnesium or manganese 3UniRule annotation
Metal bindingi878 – 8781Magnesium or manganese 4UniRule annotation
Metal bindingi880 – 8801Magnesium or manganese 4UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 21658ATPUniRule annotationAdd
BLAST
Nucleotide bindingi742 – 79958ATPUniRule annotationAdd
BLAST

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 chainUniRule annotation (EC:6.3.5.5UniRule annotation)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chainUniRule annotation
Gene namesi
Name:carBUniRule annotation
Ordered Locus Names:ZMO1617
OrganismiZymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Taxonomic identifieri264203 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeZymomonas
Proteomesi
  • UP000001173 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11121112Carbamoyl-phosphate synthase large chainPRO_0000145070Add
BLAST

Proteomic databases

PRIDEiO50236.

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.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliO50236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 330198ATP-grasp 1UniRule annotationAdd
BLAST
Domaini716 – 907192ATP-grasp 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 404404Carboxyphosphate synthetic domainAdd
BLAST
Regioni405 – 587183Oligomerization domainAdd
BLAST
Regioni588 – 972385Carbamoyl phosphate synthetic domainAdd
BLAST
Regioni973 – 1112140Allosteric 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. 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.
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. 2 hits.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O50236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKRTDLQSI MIIGAGPIVI GQACEFDYSG TQACKALREE GYRVILVNSN
60 70 80 90 100
PATIMTDPDM ADATYIEPIT PEVVARIIEK ERPDALLPTM GGQTALNTAL
110 120 130 140 150
ALASDGTLEK FNCEMIGADA TAIDKAEDRL KFRQAMDKIG LESPRSSVAH
160 170 180 190 200
SLEEALDGLD YVGLPAIIRP SFTMGGTGGG VAYNKEEFID IVSGGLSASP
210 220 230 240 250
TQEVLIEESV IGWKEYEMEV VRDRHDNCII ICSIENIDPM GVHTGDSITV
260 270 280 290 300
APALTMTDKE YQIMRNASIA VLREIGVETG NGGSNVQFAL NPENGRLVVI
310 320 330 340 350
EMNPRVSRSS ALASKATGFP IAKVATKLAI GYTLDEITND ITGATPASFE
360 370 380 390 400
PTIDYVVTKI PRFAFEKFKN AKPLLTTAMK SVGEVMAIGR SFPESLQKAL
410 420 430 440 450
RGLENGLSGL DPVEALVGAN PSVIEAELAR PTPDRLLVAA QALREGLPAE
460 470 480 490 500
KICEITHYDP WFIARLAEII AAENEVISNG LPLEAAAFRR LKAMGFSDKR
510 520 530 540 550
LADLALQSAH LRGLGKAQAK GSGIVHDALQ AMTGGVTEAE VRTLRHSLNI
560 570 580 590 600
RPVFKRIDSC AAEFEAKTPY MYSTYEAPFF GEPVCDSLPS NRKKVVILGG
610 620 630 640 650
GPNRIGQGLE FDYCCCHACF ALEAAGYETI MVNCNPETVS TDYDTSDRLY
660 670 680 690 700
FEPLTGEDVL EILHTEQKNG TLVGVIVQFG GQTPLKLAAE IEKAGIPILG
710 720 730 740 750
TSPDAIDLAE DRERFSALVS ELGLLQPANG IARSRDEAIS VADKIGYPIL
760 770 780 790 800
IRPSYVLGGR AMEIIDGPSQ LDDYIHTAVK VSGESPVLID QYLRDATEVD
810 820 830 840 850
VDAVADGDDV VVAGILQHIE EAGIHSGDSA CSIPPYSLPA SIIEEIKSQT
860 870 880 890 900
DKLARALKVQ GLMNIQFAVK GDKVYLIEVN PRASRTVPFV AKADGRPVAQ
910 920 930 940 950
VAARVMAGEK LRNLPEISWP EGYTAVKEAV FPWARFPGVD PVLSPEMKST
960 970 980 990 1000
GEVMGIDIDF PMAFAKAQLA AGNALPRAGT FFISVKDSDK AQIVEPIKAL
1010 1020 1030 1040 1050
TDLGIKLVAT DGTARYLQSK GVPVERVNKV REGRPHIVDL IKDGAISLVV
1060 1070 1080 1090 1100
NTTEGWQSLQ DSASIRSSVV LAPVPYFTTA AAAIVAAEAI VAIKARELEV
1110
RSLQSYHSMK HA
Length:1,112
Mass (Da):119,529
Last modified:February 15, 2005 - v2
Checksum:iB65A11546F8E085D
GO

Sequence cautioni

The sequence AE008692 differs from that shown. Reason: Frameshift at position 282. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631Missing in AAC70356 (Ref. 1) Curated
Sequence conflicti281 – 2822Missing in AAC70356 (Ref. 1) Curated
Sequence conflicti560 – 59132CAAEF…SLPSN → ARLNLKPKRLICIPLMKRLS LVNLFAILCQAI in AAC70356 (Ref. 1) CuratedAdd
BLAST
Sequence conflicti940 – 95617Missing in AAC70356 (Ref. 1) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086791 Genomic DNA. Translation: AAC70356.1.
AE008692 Genomic DNA. No translation available.
PIRiT33717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF086791 Genomic DNA. Translation: AAC70356.1.
AE008692 Genomic DNA. No translation available.
PIRiT33717.

3D structure databases

ProteinModelPortaliO50236.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO50236.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
UPA00070; UER00115.

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. 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.
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. 2 hits.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARB_ZYMMO
AccessioniPrimary (citable) accession number: O50236
Secondary accession number(s): Q5NM19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: February 15, 2005
Last modified: November 11, 2015
This is version 107 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.