Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q91293

- CPSM_LITCT

UniProt

Q91293 - CPSM_LITCT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Carbamoyl-phosphate synthase [ammonia], mitochondrial

Gene
N/A
Organism
Lithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell.By similarity

Catalytic activityi

2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate.

Enzyme regulationi

Requires N-acetyl-L-glutamate (NAG) as an allosteric activator.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei290 – 2901For GATase activityBy similarity
Binding sitei1388 – 13881Allosteric activatorBy similarity
Binding sitei1391 – 13911Allosteric activatorBy similarity
Binding sitei1407 – 14071Allosteric activatorBy similarity
Binding sitei1433 – 14331Allosteric activatorBy similarity
Binding sitei1436 – 14361Allosteric activatorBy similarity
Binding sitei1445 – 14451Allosteric activatorBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. carbamoyl-phosphate synthase (ammonia) activity Source: UniProtKB-EC
  3. metal ion binding Source: InterPro

GO - Biological processi

  1. carbamoyl phosphate biosynthetic process Source: InterPro
  2. glutamine catabolic process Source: InterPro
  3. urea cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Urea cycle

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase [ammonia], mitochondrial (EC:6.3.4.16)
Alternative name(s):
Carbamoyl-phosphate synthetase I
Short name:
CPSase I
OrganismiLithobates catesbeiana (American bullfrog) (Rana catesbeiana)
Taxonomic identifieri8400 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraNeobatrachiaRanoideaRanidaeRanaAquarana

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionBy similarityAdd
BLAST
Chaini34 – 14961463Carbamoyl-phosphate synthase [ammonia], mitochondrialPRO_0000029900Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ91293.
SMRiQ91293. Positions 1340-1474.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini215 – 401187Glutamine amidotransferase type-1Add
BLAST
Domaini548 – 740193ATP-grasp 1Add
BLAST
Domaini1090 – 1281192ATP-grasp 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 214181Anthranilate phosphoribosyltransferase homologAdd
BLAST

Sequence similaritiesi

Contains 2 ATP-grasp domains.Curated

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

HOVERGENiHBG000279.

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.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_01209. CPSase_S_chain.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91293-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTRILSVFKT AKTGVLNAAA HRYRGFSKAG VRLMSVKAQT ANLVLEDGTK
60 70 80 90 100
IKGYSFGHPA SVAGEVIFNT GLGGYVEAVT DPSYHGQILT LTNPIIGNGG
110 120 130 140 150
APDTKARDAY GLMKYIESEN IQASGLLVLD YSHEYSHWGA VKSLSEWLHE
160 170 180 190 200
EKVPALCGID TRMLAKKIRD NKGAVLGKIE FEGQPVEFID PNKRNLIAEV
210 220 230 240 250
STKETKVFGK GNPVRIVAVD CGVKHNIIRQ LVKRGAEVHL VPWNHDFSQM
260 270 280 290 300
EYDGLLITSG PGNPELAKPL IQNLKKVFQS DRPEPIFGIC KGNEIAALAA
310 320 330 340 350
GGKTYRLPMA NRGQNQPVMI TLNGQAFITA QNHAYAVDNN SLPAGWKPLF
360 370 380 390 400
VNINDQSNEG IMHETKPIFT SQFHPEANPG PVDTEFLFDV YMSLIKKGKG
410 420 430 440 450
TTLTSVMPKP ALQSKRIDVA KVLILGSGGL SIGQAGEFDY SGSQAVKAMK
460 470 480 490 500
EENVKTVLMN PNIASVQTNE VGLKQADTVY FLPITPQFVT EVIKAEKTDG
510 520 530 540 550
IILGMGGQTA LNCGVELFKR GVLKEYGVRV LGTSVESIMF TEDRQLFSDK
560 570 580 590 600
LNEIKEPIAP SFAVESVKDA LEAADKIGYP VMIRSAYALG GLGSGLCPDK
610 620 630 640 650
ETLTDLATKA LAMTNQILVE RSVVGWKEIE YEVVRDAADN CVTVCNMENV
660 670 680 690 700
DAMGVHTGDS IVVAPCQTLS NEECQMLRAV SIKVVRHLGI VGECNIQFAL
710 720 730 740 750
HPTSLEYVII EVNARLSRSS ALASKATGYP LAFIAAKIAL GIPLPEIKNV
760 770 780 790 800
VSGKTTACFE PSLDYMVTKI PRWDLDRFHG ASGLIGSSMK SVGEVMAIGR
810 820 830 840 850
TFEESFQKAL RMCHPSVDGF TSNLPMNKAW SSDVNLRKEM AEPTSTRMYS
860 870 880 890 900
MAKAIQSGIS LDEINKLTAI DKWFLYKMQG ILNMEKTLKG SRSESVPEET
910 920 930 940 950
LRRAKQIGFS DRYIGKCLGL SETQTRELRL NKNVKPWVKQ IDTLAAEYPA
960 970 980 990 1000
ITNYLYLTYN GQEHDIKFDD HGMMVLGCGP YHIGSSVEFD WCAVSSIRTL
1010 1020 1030 1040 1050
RHVGKKTVVV NCNPETVSTD FDECDKLYFE ELSQERIMDV FQLEQCDGCI
1060 1070 1080 1090 1100
ISVGGQIPNN LAVPLYKNGV KIMGTSPMQI DRAEDRSIFS AVLDELQIAQ
1110 1120 1130 1140 1150
APWKAVNSLD DALQFTKTVG YPCLLRPSYV LSGSAMNVVY GEEELKTFLA
1160 1170 1180 1190 1200
EATRVSQEHP VVITKFIEGA REVEMDAVGK EGRVISHAIS EHVEDAGVHS
1210 1220 1230 1240 1250
GDATLMIPTQ SISQGAIEKV KIATKKIATA FAISGPFNVQ FLVRGNDVLV
1260 1270 1280 1290 1300
IECNLRASRS FPFVSKTLGV DFIDVATKVM IGEKIDESSL PTLERPVIPA
1310 1320 1330 1340 1350
DYVGIKAPMF SWPRLRGADP VLKCEMASTG EVACFGQNVY SAFLKAMIST
1360 1370 1380 1390 1400
GFKLPQKGIL IGIQHSFRPH FLGTAQTLKD EGFKLYATEA TADWLNANDI
1410 1420 1430 1440 1450
TATPVAWPSQ EGQSGPSSIY KLIKEGNIDM VINLPNNNTK YVRDNFAIRR
1460 1470 1480 1490
TAVDTGTALL TNFQVVKMFA EAIKYSGDLD AKSLFHYRQF GGAKPS
Length:1,496
Mass (Da):163,767
Last modified:November 1, 1996 - v1
Checksum:i2360BF05D21B059E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05193 mRNA. Translation: AAA19016.1.
PIRiI51170.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05193 mRNA. Translation: AAA19016.1 .
PIRi I51170.

3D structure databases

ProteinModelPortali Q91293.
SMRi Q91293. Positions 1340-1474.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG000279.

Family and domain databases

Gene3Di 1.10.1030.10. 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.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPi MF_01209. CPSase_S_chain.
InterProi IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view ]
Pfami PF00289. CPSase_L_chain. 2 hits.
PF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
PF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PRINTSi PR00098. CPSASE.
SMARTi SM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF48108. SSF48108. 1 hit.
SSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
SSF52335. SSF52335. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsi TIGR01369. CPSaseII_lrg. 1 hit.
TIGR01368. CPSaseIIsmall. 1 hit.
PROSITEi PS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "3,5,3'-Triiodothyronine-induced carbamyl-phosphate synthetase gene expression is stabilized in the liver of Rana catesbeiana tadpoles during heat shock."
    Helbing C.C., Atkinson B.G.
    J. Biol. Chem. 269:11743-11750(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.

Entry informationi

Entry nameiCPSM_LITCT
AccessioniPrimary (citable) accession number: Q91293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3