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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi385 – 3851Copper
Metal bindingi757 – 7571Molybdenum

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 803803Carbon monoxide dehydrogenase large chainPRO_0000079809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei384 – 38414-hydroxyarginine1 Publication

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

1
803
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 158Combined sources
Helixi27 – 304Combined sources
Turni31 – 333Combined sources
Helixi38 – 403Combined sources
Beta strandi47 – 537Combined sources
Beta strandi55 – 6511Combined sources
Helixi67 – 715Combined sources
Beta strandi75 – 795Combined sources
Helixi81 – 844Combined sources
Helixi85 – 873Combined sources
Beta strandi90 – 934Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi114 – 1229Combined sources
Helixi123 – 13210Combined sources
Beta strandi134 – 1396Combined sources
Helixi146 – 1494Combined sources
Helixi159 – 1613Combined sources
Beta strandi168 – 1714Combined sources
Beta strandi177 – 1848Combined sources
Helixi186 – 19510Combined sources
Beta strandi197 – 20610Combined sources
Beta strandi218 – 2247Combined sources
Turni225 – 2284Combined sources
Beta strandi229 – 2346Combined sources
Helixi239 – 25012Combined sources
Helixi254 – 2563Combined sources
Beta strandi257 – 2604Combined sources
Turni268 – 2714Combined sources
Helixi276 – 28813Combined sources
Beta strandi292 – 2954Combined sources
Helixi298 – 3047Combined sources
Beta strandi311 – 3199Combined sources
Beta strandi325 – 33511Combined sources
Turni349 – 3524Combined sources
Helixi353 – 3553Combined sources
Turni356 – 3594Combined sources
Beta strandi363 – 37210Combined sources
Beta strandi379 – 3813Combined sources
Turni386 – 3883Combined sources
Helixi389 – 40719Combined sources
Helixi413 – 4186Combined sources
Helixi422 – 4243Combined sources
Beta strandi426 – 4283Combined sources
Helixi440 – 45112Combined sources
Helixi453 – 46513Combined sources
Beta strandi470 – 48112Combined sources
Turni489 – 4913Combined sources
Beta strandi497 – 4993Combined sources
Beta strandi501 – 5077Combined sources
Beta strandi513 – 5186Combined sources
Beta strandi522 – 5243Combined sources
Helixi526 – 53813Combined sources
Helixi542 – 5443Combined sources
Beta strandi545 – 5484Combined sources
Turni552 – 5543Combined sources
Helixi566 – 59227Combined sources
Helixi597 – 5993Combined sources
Beta strandi600 – 6023Combined sources
Beta strandi604 – 6118Combined sources
Beta strandi616 – 6183Combined sources
Helixi619 – 62810Combined sources
Beta strandi636 – 6449Combined sources
Beta strandi653 – 66311Combined sources
Turni664 – 6663Combined sources
Beta strandi669 – 67911Combined sources
Helixi686 – 70520Combined sources
Turni722 – 7243Combined sources
Turni730 – 7323Combined sources
Beta strandi737 – 7404Combined sources
Helixi758 – 77518Combined sources
Helixi776 – 7783Combined sources
Helixi789 – 79810Combined sources

3D structure databases

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

Publicationsi

  1. "Cloning and molecular characterization of the genes for carbon monoxide dehydrogenase and localization of molybdopterin, flavin adenine dinucleotide, and iron-sulfur centers in the enzyme of Hydrogenophaga pseudoflava."
    Kang B.S., Kim Y.M.
    J. Bacteriol. 181:5581-5590(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], COFACTOR, SUBUNIT.
  2. "Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria."
    Kraut M., Hugendieck I., Herwig S., Meyer O.
    Arch. Microbiol. 152:335-341(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-9.
  3. "The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase."
    Haenzelmann P., Dobbek H., Gremer L., Huber R., Meyer O.
    J. Mol. Biol. 301:1221-1235(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), HYDROXYLATION AT ARG-384.
  4. "The role of Se, Mo and Fe in the structure and function of carbon monoxide dehydrogenase."
    Meyer O., Gremer L., Ferner R., Ferner M., Dobbek H., Gnida M., Meyer-Klaucke W., Huber R.
    Biol. Chem. 381:865-876(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

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: July 6, 2016
This is version 80 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.