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Protein

Carbon monoxide dehydrogenase large chain

Gene

cutL

Organism
Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of carbon monoxide to carbon dioxide.By similarity

Catalytic activityi

CO + a quinone + H2O = CO2 + a quinol.By similarity

Cofactori

Protein has several cofactor binding sites:
  • Cu+1 PublicationNote: Binds 1 Cu+ ion per subunit.1 Publication
  • Mo-molybdopterin cytosine dinucleotide1 PublicationNote: Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi385Copper1
Metal bindingi757Molybdenum1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Molybdenum

Enzyme and pathway databases

BRENDAi1.2.2.4. 2729.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbon monoxide dehydrogenase large chain (EC:1.2.5.3By similarity)
Short name:
CO dehydrogenase subunit L
Short name:
CO-DH L
Gene namesi
Name:cutL
OrganismiHydrogenophaga pseudoflava (Pseudomonas carboxydoflava)
Taxonomic identifieri47421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeHydrogenophaga

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000798091 – 803Carbon monoxide dehydrogenase large chainAdd BLAST803

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3844-hydroxyarginine1 Publication1

Keywords - PTMi

Hydroxylation

Interactioni

Subunit structurei

Dimer of heterotrimers. Each heterotrimer consists of a large, a medium and a small subunit.1 Publication

Structurei

Secondary structure

1803
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 15Combined sources8
Helixi27 – 30Combined sources4
Turni31 – 33Combined sources3
Helixi38 – 40Combined sources3
Beta strandi47 – 53Combined sources7
Beta strandi55 – 65Combined sources11
Helixi67 – 71Combined sources5
Beta strandi75 – 79Combined sources5
Helixi81 – 84Combined sources4
Helixi85 – 87Combined sources3
Beta strandi90 – 93Combined sources4
Beta strandi99 – 103Combined sources5
Beta strandi106 – 108Combined sources3
Beta strandi114 – 122Combined sources9
Helixi123 – 132Combined sources10
Beta strandi134 – 139Combined sources6
Helixi146 – 149Combined sources4
Helixi159 – 161Combined sources3
Beta strandi168 – 171Combined sources4
Beta strandi177 – 184Combined sources8
Helixi186 – 195Combined sources10
Beta strandi197 – 206Combined sources10
Beta strandi218 – 224Combined sources7
Turni225 – 228Combined sources4
Beta strandi229 – 234Combined sources6
Helixi239 – 250Combined sources12
Helixi254 – 256Combined sources3
Beta strandi257 – 260Combined sources4
Turni268 – 271Combined sources4
Helixi276 – 288Combined sources13
Beta strandi292 – 295Combined sources4
Helixi298 – 304Combined sources7
Beta strandi311 – 319Combined sources9
Beta strandi325 – 335Combined sources11
Turni349 – 352Combined sources4
Helixi353 – 355Combined sources3
Turni356 – 359Combined sources4
Beta strandi363 – 372Combined sources10
Beta strandi379 – 381Combined sources3
Turni386 – 388Combined sources3
Helixi389 – 407Combined sources19
Helixi413 – 418Combined sources6
Helixi422 – 424Combined sources3
Beta strandi426 – 428Combined sources3
Helixi440 – 451Combined sources12
Helixi453 – 465Combined sources13
Beta strandi470 – 481Combined sources12
Turni489 – 491Combined sources3
Beta strandi497 – 499Combined sources3
Beta strandi501 – 507Combined sources7
Beta strandi513 – 518Combined sources6
Beta strandi522 – 524Combined sources3
Helixi526 – 538Combined sources13
Helixi542 – 544Combined sources3
Beta strandi545 – 548Combined sources4
Turni552 – 554Combined sources3
Helixi566 – 592Combined sources27
Helixi597 – 599Combined sources3
Beta strandi600 – 602Combined sources3
Beta strandi604 – 611Combined sources8
Beta strandi616 – 618Combined sources3
Helixi619 – 628Combined sources10
Beta strandi636 – 644Combined sources9
Beta strandi653 – 663Combined sources11
Turni664 – 666Combined sources3
Beta strandi669 – 679Combined sources11
Helixi686 – 705Combined sources20
Turni722 – 724Combined sources3
Turni730 – 732Combined sources3
Beta strandi737 – 740Combined sources4
Helixi758 – 775Combined sources18
Helixi776 – 778Combined sources3
Helixi789 – 798Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFUX-ray2.35B/E1-803[»]
1FFVX-ray2.25B/E1-803[»]
ProteinModelPortaliP19913.
SMRiP19913.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19913.

Family & Domainsi

Family and domain databases

Gene3Di3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProiIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012780. CO_Mo_DH_lsu.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
TIGRFAMsiTIGR02416. CO_dehy_Mo_lg. 1 hit.

Sequencei

Sequence statusi: Complete.

P19913-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAPVQDAEA RELALAGMRP RACAKEDARF IQGKGNYVDD IKMPGMLHMD
60 70 80 90 100
IVRAPIAHGR IKKIHKDAAL AMPGVHAVLT AEDLKPLKLH WMPTLAGDVA
110 120 130 140 150
AVLADEKVHF QMQEVAIVIA DDRYIAADAV EAVKVEYDEL PVVIDPIDAL
160 170 180 190 200
KPDAPVLRED LAGKTSGAHG PREHHNHIFT WGAGDKAATD AVFANAPVTV
210 220 230 240 250
SQHMYYPRVH PCPLETCGCV ASFDPIKGDL TTYITSQAPH VVRTVVSMLS
260 270 280 290 300
GIPESKVRIV SPDIGGGFGN KVGIYPGYVC AIVASIVLGR PVKWVEDRVE
310 320 330 340 350
NISTTAFARD YHMDGELAAT PDGKILGLRV NVVADHGAFD ACADPTKFPA
360 370 380 390 400
GLFHICSGSY DIPRAHCSVK GVYTNKAPGG VAYRCSFRVT EAVYLIERMV
410 420 430 440 450
DVLAQKLNMD KAEIRAKNFI RKEQFPYTTQ FGFEYDSGDY HTALKKVLDA
460 470 480 490 500
VDYPAWRAEQ AARRADPNSP TLMGIGLVTF TEVVGAGPSK MCDILGVGMF
510 520 530 540 550
DSCEIRIHPT GSAIARMGTI TQGQGHQTTY AQIIATELGI PSEVIQVEEG
560 570 580 590 600
DTSTAPYGLG TYGSRSTPVA GAAIALAARK IHAKARKIAA HMLEVNENDL
610 620 630 640 650
DWEVDRFKVK GDDSKFKTMA DIAWQAYHQP PAGLEPGLEA VHYYDPPNFT
660 670 680 690 700
YPFGIYLCVV DIDRATGETK VRRFYALDDC GTRINPMIIE GQIHGGLTEG
710 720 730 740 750
YAVAMGQQMP FDAQGNLLGN TLMDYFLPTA VETPHWETDH TVTPSPHHPI
760 770 780 790 800
GAKGVAESPH VGSIPTFTAA VVDAFAHVGV THLDMPHTSY RVWKSLKEHN

LAL
Length:803
Mass (Da):87,229
Last modified:July 11, 2002 - v2
Checksum:i3CD5FE205DBE0712
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80806 Genomic DNA. Translation: AAD00363.1.
PIRiPL0139.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U80806 Genomic DNA. Translation: AAD00363.1.
PIRiPL0139.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FFUX-ray2.35B/E1-803[»]
1FFVX-ray2.25B/E1-803[»]
ProteinModelPortaliP19913.
SMRiP19913.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.2.2.4. 2729.

Miscellaneous databases

EvolutionaryTraceiP19913.

Family and domain databases

Gene3Di3.30.365.10. 6 hits.
3.90.1170.50. 1 hit.
InterProiIPR000674. Ald_Oxase/Xan_DH_a/b.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012780. CO_Mo_DH_lsu.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
[Graphical view]
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF54665. SSF54665. 1 hit.
SSF56003. SSF56003. 1 hit.
TIGRFAMsiTIGR02416. CO_dehy_Mo_lg. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDCML_HYDPS
AccessioniPrimary (citable) accession number: P19913
Secondary accession number(s): Q9RBR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2002
Last modified: November 2, 2016
This is version 82 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

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.