DCML_AFIC5
ID DCML_AFIC5 Reviewed; 809 AA.
AC P19919; F8C0Z6; Q51325;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Carbon monoxide dehydrogenase large chain;
DE Short=CO dehydrogenase subunit L;
DE Short=CO-DH L;
DE EC=1.2.5.3 {ECO:0000269|PubMed:12475995, ECO:0000269|PubMed:21275368};
GN Name=coxL; OrderedLocusNames=OCA5_pHCG300310;
OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
OS (Oligotropha carboxidovorans).
OG Plasmid megaplasmid pHCG3.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Afipia.
OX NCBI_TaxID=504832;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=7721710; DOI=10.1128/jb.177.8.2197-2203.1995;
RA Schuebel U., Kraut M., Moersdorf G., Meyer O.;
RT "Molecular characterization of the gene cluster coxMSL encoding the
RT molybdenum-containing carbon monoxide dehydrogenase of Oligotropha
RT carboxidovorans.";
RL J. Bacteriol. 177:2197-2203(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=14644498; DOI=10.1016/j.gene.2003.08.027;
RA Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.;
RT "Complete nucleotide sequence of the circular megaplasmid pHCG3 of
RT Oligotropha carboxidovorans: function in the chemolithoautotrophic
RT utilization of CO, H(2) and CO(2).";
RL Gene 322:67-75(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5;
RX PubMed=21742883; DOI=10.1128/jb.05619-11;
RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA Meyer O.;
RT "Complete genome sequences of the chemolithoautotrophic Oligotropha
RT carboxidovorans strains OM4 and OM5.";
RL J. Bacteriol. 193:5043-5043(2011).
RN [4]
RP PROTEIN SEQUENCE OF 1-13.
RX PubMed=2818128; DOI=10.1007/bf00425170;
RA Kraut M., Hugendieck I., Herwig S., Meyer O.;
RT "Homology and distribution of CO dehydrogenase structural genes in
RT carboxydotrophic bacteria.";
RL Arch. Microbiol. 152:335-341(1989).
RN [5]
RP COFACTOR.
RX PubMed=12515558; DOI=10.1021/bi026514n;
RA Gnida M., Ferner R., Gremer L., Meyer O., Meyer-Klaucke W.;
RT "A novel binuclear [CuSMo] cluster at the active site of carbon monoxide
RT dehydrogenase: characterization by X-ray absorption spectroscopy.";
RL Biochemistry 42:222-230(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21275368; DOI=10.1021/bi1017182;
RA Wilcoxen J., Zhang B., Hille R.;
RT "Reaction of the molybdenum- and copper-containing carbon monoxide
RT dehydrogenase from Oligotropha carboxydovorans with quinones.";
RL Biochemistry 50:1910-1916(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CODH MEDIUM AND SMALL
RP SUBUNITS; COPPER AND MOLYBDOPTERIN CYTOSINE DINUCLEOTIDE, COFACTOR, AND
RP SUBUNIT.
RX PubMed=10430865; DOI=10.1073/pnas.96.16.8884;
RA Dobbek H., Gremer L., Meyer O., Huber R.;
RT "Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur
RT flavoprotein containing S-selanylcysteine.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8884-8889(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.09 ANGSTROMS) IN COMPLEX WITH CODH MEDIUM AND
RP SMALL SUBUNITS; COPPER AND MOLYBDOPTERIN CYTOSINE DINUCLEOTIDE, FUNCTION,
RP COFACTOR, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=12475995; DOI=10.1073/pnas.212640899;
RA Dobbek H., Gremer L., Kiefersauer R., Huber R., Meyer O.;
RT "Catalysis at a dinuclear CuSMo(==O)OH cluster in a CO dehydrogenase
RT resolved at 1.1-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15971-15976(2002).
CC -!- FUNCTION: Catalyzes the oxidation of carbon monoxide to carbon dioxide.
CC {ECO:0000269|PubMed:12475995, ECO:0000269|PubMed:21275368}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + CO + H2O = a quinol + CO2; Xref=Rhea:RHEA:48880,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245,
CC ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.2.5.3;
CC Evidence={ECO:0000269|PubMed:12475995, ECO:0000269|PubMed:21275368};
CC -!- COFACTOR:
CC Name=Cu(+); Xref=ChEBI:CHEBI:49552;
CC Evidence={ECO:0000269|PubMed:12475995, ECO:0000269|PubMed:12515558};
CC Note=Binds 1 Cu(+) ion per subunit. {ECO:0000269|PubMed:12475995,
CC ECO:0000269|PubMed:12515558};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin cytosine dinucleotide; Xref=ChEBI:CHEBI:71308;
CC Evidence={ECO:0000269|PubMed:10430865, ECO:0000269|PubMed:12475995,
CC ECO:0000269|PubMed:12515558};
CC Note=Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor
CC per subunit. {ECO:0000269|PubMed:10430865, ECO:0000269|PubMed:12475995,
CC ECO:0000269|PubMed:12515558};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.4 uM for 1,4-benzoquinone {ECO:0000269|PubMed:21275368};
CC -!- SUBUNIT: Dimer of heterotrimers. Each heterotrimer consists of a large,
CC a medium and a small subunit. {ECO:0000269|PubMed:10430865}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002827; AEI08106.1; -; Genomic_DNA.
DR PIR; C56279; C56279.
DR RefSeq; WP_013913730.1; NC_015689.1.
DR PDB; 1N5W; X-ray; 1.50 A; B/E=1-809.
DR PDB; 1N60; X-ray; 1.19 A; B/E=1-809.
DR PDB; 1N61; X-ray; 1.30 A; B/E=1-809.
DR PDB; 1N62; X-ray; 1.09 A; B/E=1-809.
DR PDB; 1N63; X-ray; 1.21 A; B/E=1-809.
DR PDB; 1ZXI; X-ray; 1.70 A; B/E=1-809.
DR PDBsum; 1N5W; -.
DR PDBsum; 1N60; -.
DR PDBsum; 1N61; -.
DR PDBsum; 1N62; -.
DR PDBsum; 1N63; -.
DR PDBsum; 1ZXI; -.
DR AlphaFoldDB; P19919; -.
DR SMR; P19919; -.
DR EnsemblBacteria; AEI08106; AEI08106; OCA5_pHCG300310.
DR KEGG; ocg:OCA5_pHCG300310; -.
DR PATRIC; fig|504832.7.peg.3606; -.
DR HOGENOM; CLU_001681_2_0_5; -.
DR OMA; CTHNPLG; -.
DR OrthoDB; 117507at2; -.
DR BioCyc; MetaCyc:MON-19674; -.
DR BRENDA; 1.2.5.3; 4399.
DR BRENDA; 1.2.7.4; 4399.
DR SABIO-RK; P19919; -.
DR EvolutionaryTrace; P19919; -.
DR Proteomes; UP000007730; Plasmid pHCG3.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:InterPro.
DR GO; GO:0008805; F:carbon-monoxide oxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012780; CO_Mo_DH_lsu.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR TIGRFAMs; TIGR02416; CO_dehy_Mo_lg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Metal-binding; Molybdenum;
KW Oxidoreductase; Plasmid; Reference proteome.
FT CHAIN 1..809
FT /note="Carbon monoxide dehydrogenase large chain"
FT /id="PRO_0000079810"
FT BINDING 388
FT /ligand="Cu(+)"
FT /ligand_id="ChEBI:CHEBI:49552"
FT /evidence="ECO:0000269|PubMed:12475995"
FT BINDING 763
FT /ligand="Mo-molybdopterin cytosine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71308"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000269|PubMed:10430865,
FT ECO:0000269|PubMed:12475995"
FT CONFLICT 6
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 11..12
FT /note="SA -> AG (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 11..18
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 279..291
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 301..307
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 314..322
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 328..338
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 392..410
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 443..454
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 456..471
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 476..487
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 507..513
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 519..524
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 532..544
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 572..575
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 576..599
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 603..605
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 606..608
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 610..615
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 618..624
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 625..634
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 642..650
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 659..669
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 675..685
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 692..711
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 728..730
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 736..738
FT /evidence="ECO:0007829|PDB:1N62"
FT STRAND 743..746
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 764..782
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 783..785
FT /evidence="ECO:0007829|PDB:1N62"
FT HELIX 795..804
FT /evidence="ECO:0007829|PDB:1N62"
FT TURN 805..808
FT /evidence="ECO:0007829|PDB:1N62"
SQ SEQUENCE 809 AA; 88739 MW; 7F2F3D0EC996BDBD CRC64;
MNIQTTVEPT SAERAEKLQG MGCKRKRVED IRFTQGKGNY VDDVKLPGML FGDFVRSSHA
HARIKSIDTS KAKALPGVFA VLTAADLKPL NLHYMPTLAG DVQAVLADEK VLFQNQEVAF
VVAKDRYVAA DAIELVEVDY EPLPVLVDPF KAMEPDAPLL REDIKDKMTG AHGARKHHNH
IFRWEIGDKE GTDATFAKAE VVSKDMFTYH RVHPSPLETC QCVASMDKIK GELTLWGTFQ
APHVIRTVVS LISGLPEHKI HVIAPDIGGG FGNKVGAYSG YVCAVVASIV LGVPVKWVED
RMENLSTTSF ARDYHMTTEL AATKDGKILA MRCHVLADHG AFDACADPSK WPAGFMNICT
GSYDMPVAHL AVDGVYTNKA SGGVAYRCSF RVTEAVYAIE RAIETLAQRL EMDSADLRIK
NFIQPEQFPY MAPLGWEYDS GNYPLAMKKA MDTVGYHQLR AEQKAKQEAF KRGETREIMG
IGISFFTEIV GAGPSKNCDI LGVSMFDSAE IRIHPTGSVI ARMGTKSQGQ GHETTYAQII
ATELGIPADD IMIEEGNTDT APYGLGTYGS RSTPTAGAAT AVAARKIKAK AQMIAAHMLE
VHEGDLEWDV DRFRVKGLPE KFKTMKELAW ASYNSPPPNL EPGLEAVNYY DPPNMTYPFG
AYFCIMDIDV DTGVAKTRRF YALDDCGTRI NPMIIEGQVH GGLTEAFAVA MGQEIRYDEQ
GNVLGASFMD FFLPTAVETP KWETDYTVTP SPHHPIGAKG VGESPHVGGV PCFSNAVNDA
YAFLNAGHIQ MPHDAWRLWK VGEQLGLHV
