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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: -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. no protein annotated in this organism
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 bindingi287Magnesium or manganese 1UniRule annotation1
Metal bindingi301Magnesium or manganese 1UniRule annotation1
Metal bindingi301Magnesium or manganese 2UniRule annotation1
Metal bindingi303Magnesium or manganese 2UniRule annotation1
Metal bindingi866Magnesium or manganese 3UniRule annotation1
Metal bindingi878Magnesium or manganese 3UniRule annotation1
Metal bindingi878Magnesium or manganese 4UniRule annotation1
Metal bindingi880Magnesium or manganese 4UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi159 – 216ATPUniRule annotationAdd BLAST58
Nucleotide bindingi742 – 799ATPUniRule annotationAdd BLAST58

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis, Pyrimidine biosynthesis
LigandATP-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)DescriptionActionsGraphical viewLength
ChainiPRO_00001450701 – 1112Carbamoyl-phosphate synthase large chainAdd BLAST1112

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
SMRiO50236
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini133 – 330ATP-grasp 1UniRule annotationAdd BLAST198
Domaini716 – 907ATP-grasp 2UniRule annotationAdd BLAST192
Domaini973 – 1112MGS-likePROSITE-ProRule annotationAdd BLAST140

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 404Carboxyphosphate synthetic domainAdd BLAST404
Regioni405 – 587Oligomerization domainAdd BLAST183
Regioni588 – 972Carbamoyl phosphate synthetic domainAdd BLAST385
Regioni973 – 1112Allosteric domainAdd BLAST140

Sequence similaritiesi

Belongs to the CarB family.UniRule annotation

Keywords - Domaini

Repeat

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, 2 hits
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, 1 hit
PS00867 CPSASE_2, 2 hits
PS51855 MGS, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti163Missing in AAC70356 (Ref. 1) Curated1
Sequence conflicti281 – 282Missing in AAC70356 (Ref. 1) Curated2
Sequence conflicti560 – 591CAAEF…SLPSN → ARLNLKPKRLICIPLMKRLS LVNLFAILCQAI in AAC70356 (Ref. 1) CuratedAdd BLAST32
Sequence conflicti940 – 956Missing in AAC70356 (Ref. 1) CuratedAdd BLAST17

Sequence databases

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

Similar proteinsi

Entry informationi

Entry nameiCARB_ZYMMO
AccessioniPrimary (citable) accession number: O50236
Secondary accession number(s): Q5NM19
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: February 15, 2005
Last modified: March 28, 2018
This is version 115 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health