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Protein

Carbon monoxide dehydrogenase large chain

Gene

coxL

Organism
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
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.

Catalytic activityi

CO + H2O + A = CO2 + AH2.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi388 – 3881Copper
Metal bindingi763 – 7631Molybdenum

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Metal-binding, Molybdenum

Enzyme and pathway databases

BioCyciOCAR504832:GJPZ-3598-MONOMER.
BRENDAi1.2.99.2. 4399.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbon monoxide dehydrogenase large chain (EC:1.2.99.2)
Short name:
CO dehydrogenase subunit L
Short name:
CO-DH L
Gene namesi
Name:coxL
Ordered Locus Names:OCA5_pHCG300310
Encoded oniPlasmid megaplasmid pHCG30 Publication
OrganismiOligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5)
Taxonomic identifieri504832 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeOligotropha
Proteomesi
  • UP000007730 Componenti: Plasmid pHCG3

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 809809Carbon monoxide dehydrogenase large chainPRO_0000079810Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
809
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 188Combined sources
Helixi30 – 334Combined sources
Turni34 – 363Combined sources
Helixi41 – 433Combined sources
Beta strandi50 – 567Combined sources
Beta strandi60 – 689Combined sources
Helixi70 – 745Combined sources
Beta strandi78 – 836Combined sources
Helixi84 – 874Combined sources
Helixi88 – 903Combined sources
Beta strandi93 – 964Combined sources
Beta strandi100 – 1067Combined sources
Beta strandi108 – 1114Combined sources
Beta strandi117 – 1259Combined sources
Helixi126 – 13510Combined sources
Beta strandi137 – 1426Combined sources
Helixi149 – 1513Combined sources
Helixi162 – 1643Combined sources
Beta strandi180 – 1878Combined sources
Helixi189 – 19810Combined sources
Beta strandi200 – 20910Combined sources
Beta strandi221 – 2277Combined sources
Turni228 – 2314Combined sources
Beta strandi232 – 2376Combined sources
Helixi242 – 25312Combined sources
Helixi257 – 2593Combined sources
Beta strandi260 – 2634Combined sources
Turni271 – 2744Combined sources
Helixi279 – 29113Combined sources
Beta strandi295 – 2984Combined sources
Helixi301 – 3077Combined sources
Beta strandi314 – 3229Combined sources
Beta strandi328 – 33811Combined sources
Turni352 – 3554Combined sources
Helixi356 – 3583Combined sources
Turni359 – 3624Combined sources
Beta strandi368 – 3758Combined sources
Beta strandi382 – 3843Combined sources
Turni389 – 3913Combined sources
Helixi392 – 41019Combined sources
Helixi414 – 4218Combined sources
Helixi425 – 4273Combined sources
Beta strandi429 – 4313Combined sources
Helixi443 – 45412Combined sources
Helixi456 – 47116Combined sources
Beta strandi476 – 48712Combined sources
Turni495 – 4973Combined sources
Beta strandi507 – 5137Combined sources
Beta strandi519 – 5246Combined sources
Beta strandi528 – 5303Combined sources
Helixi532 – 54413Combined sources
Helixi548 – 5503Combined sources
Beta strandi551 – 5544Combined sources
Turni558 – 5603Combined sources
Turni572 – 5754Combined sources
Helixi576 – 59924Combined sources
Helixi603 – 6053Combined sources
Beta strandi606 – 6083Combined sources
Beta strandi610 – 6156Combined sources
Beta strandi618 – 6247Combined sources
Helixi625 – 63410Combined sources
Beta strandi642 – 6509Combined sources
Beta strandi659 – 66911Combined sources
Turni670 – 6723Combined sources
Beta strandi675 – 68511Combined sources
Helixi692 – 71120Combined sources
Beta strandi723 – 7253Combined sources
Turni728 – 7303Combined sources
Turni736 – 7383Combined sources
Beta strandi743 – 7464Combined sources
Helixi764 – 78219Combined sources
Turni783 – 7853Combined sources
Helixi795 – 80410Combined sources
Turni805 – 8084Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N5WX-ray1.50B/E1-809[»]
1N60X-ray1.19B/E1-809[»]
1N61X-ray1.30B/E1-809[»]
1N62X-ray1.09B/E1-809[»]
1N63X-ray1.21B/E1-809[»]
1ZXIX-ray1.70B/E1-809[»]
ProteinModelPortaliP19919.
SMRiP19919. Positions 5-809.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19919.

Family & Domainsi

Phylogenomic databases

KOiK03520.
OMAiDPPNLTF.

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.

P19919-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIQTTVEPT SAERAEKLQG MGCKRKRVED IRFTQGKGNY VDDVKLPGML
60 70 80 90 100
FGDFVRSSHA HARIKSIDTS KAKALPGVFA VLTAADLKPL NLHYMPTLAG
110 120 130 140 150
DVQAVLADEK VLFQNQEVAF VVAKDRYVAA DAIELVEVDY EPLPVLVDPF
160 170 180 190 200
KAMEPDAPLL REDIKDKMTG AHGARKHHNH IFRWEIGDKE GTDATFAKAE
210 220 230 240 250
VVSKDMFTYH RVHPSPLETC QCVASMDKIK GELTLWGTFQ APHVIRTVVS
260 270 280 290 300
LISGLPEHKI HVIAPDIGGG FGNKVGAYSG YVCAVVASIV LGVPVKWVED
310 320 330 340 350
RMENLSTTSF ARDYHMTTEL AATKDGKILA MRCHVLADHG AFDACADPSK
360 370 380 390 400
WPAGFMNICT GSYDMPVAHL AVDGVYTNKA SGGVAYRCSF RVTEAVYAIE
410 420 430 440 450
RAIETLAQRL EMDSADLRIK NFIQPEQFPY MAPLGWEYDS GNYPLAMKKA
460 470 480 490 500
MDTVGYHQLR AEQKAKQEAF KRGETREIMG IGISFFTEIV GAGPSKNCDI
510 520 530 540 550
LGVSMFDSAE IRIHPTGSVI ARMGTKSQGQ GHETTYAQII ATELGIPADD
560 570 580 590 600
IMIEEGNTDT APYGLGTYGS RSTPTAGAAT AVAARKIKAK AQMIAAHMLE
610 620 630 640 650
VHEGDLEWDV DRFRVKGLPE KFKTMKELAW ASYNSPPPNL EPGLEAVNYY
660 670 680 690 700
DPPNMTYPFG AYFCIMDIDV DTGVAKTRRF YALDDCGTRI NPMIIEGQVH
710 720 730 740 750
GGLTEAFAVA MGQEIRYDEQ GNVLGASFMD FFLPTAVETP KWETDYTVTP
760 770 780 790 800
SPHHPIGAKG VGESPHVGGV PCFSNAVNDA YAFLNAGHIQ MPHDAWRLWK

VGEQLGLHV
Length:809
Mass (Da):88,739
Last modified:July 11, 2002 - v2
Checksum:i7F2F3D0EC996BDBD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61Missing AA sequence (PubMed:2818128).Curated
Sequence conflicti11 – 122SA → AG AA sequence (PubMed:2818128).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002827 Genomic DNA. Translation: AEI08106.1.
PIRiC56279.
RefSeqiWP_013913730.1. NC_015689.1.

Genome annotation databases

EnsemblBacteriaiAEI08106; AEI08106; OCA5_pHCG300310.
KEGGiocg:OCA5_pHCG300310.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002827 Genomic DNA. Translation: AEI08106.1.
PIRiC56279.
RefSeqiWP_013913730.1. NC_015689.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N5WX-ray1.50B/E1-809[»]
1N60X-ray1.19B/E1-809[»]
1N61X-ray1.30B/E1-809[»]
1N62X-ray1.09B/E1-809[»]
1N63X-ray1.21B/E1-809[»]
1ZXIX-ray1.70B/E1-809[»]
ProteinModelPortaliP19919.
SMRiP19919. Positions 5-809.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAEI08106; AEI08106; OCA5_pHCG300310.
KEGGiocg:OCA5_pHCG300310.

Phylogenomic databases

KOiK03520.
OMAiDPPNLTF.

Enzyme and pathway databases

BioCyciOCAR504832:GJPZ-3598-MONOMER.
BRENDAi1.2.99.2. 4399.

Miscellaneous databases

EvolutionaryTraceiP19919.

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

« Hide 'large scale' publications
  1. "Molecular characterization of the gene cluster coxMSL encoding the molybdenum-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans."
    Schuebel U., Kraut M., Moersdorf G., Meyer O.
    J. Bacteriol. 177:2197-2203(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 49405 / DSM 1227 / OM5.
  2. "Complete nucleotide sequence of the circular megaplasmid pHCG3 of Oligotropha carboxidovorans: function in the chemolithoautotrophic utilization of CO, H(2) and CO(2)."
    Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.
    Gene 322:67-75(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49405 / DSM 1227 / OM5.
  3. "Complete genome sequences of the chemolithoautotrophic Oligotropha carboxidovorans strains OM4 and OM5."
    Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., Meyer O.
    J. Bacteriol. 193:5043-5043(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 49405 / DSM 1227 / OM5.
  4. "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 1-13.
  5. "A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: characterization by X-ray absorption spectroscopy."
    Gnida M., Ferner R., Gremer L., Meyer O., Meyer-Klaucke W.
    Biochemistry 42:222-230(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR.
  6. "Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine."
    Dobbek H., Gremer L., Meyer O., Huber R.
    Proc. Natl. Acad. Sci. U.S.A. 96:8884-8889(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  7. "Catalysis at a dinuclear CuSMo(==O)OH cluster in a CO dehydrogenase resolved at 1.1-A resolution."
    Dobbek H., Gremer L., Kiefersauer R., Huber R., Meyer O.
    Proc. Natl. Acad. Sci. U.S.A. 99:15971-15976(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS).

Entry informationi

Entry nameiDCML_OLICO
AccessioniPrimary (citable) accession number: P19919
Secondary accession number(s): F8C0Z6, Q51325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2002
Last modified: December 9, 2015
This is version 106 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, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

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.